D-Stereoisomer preference of the OmpA-like domain of Pal in peptidoglycan of Acinetobacter baumannii

Kwon Joo Yeo; Woo Cheol Lee; Saeyoung Lee; Eunha Hwang; Jeong Soon Park; In Geol Choi; Seung Il Kim; Je Chul Lee; Young Ho Jeon; Chaejoon Cheong; Hye Yeon Kim

doi:10.1016/j.procbio.2017.01.009

D-Stereoisomer preference of the OmpA-like domain of Pal in peptidoglycan of Acinetobacter baumannii

Kwon Joo Yeo, Woo Cheol Lee, Saeyoung Lee, Eunha Hwang, Jeong Soon Park, In Geol Choi, Seung Il Kim, Je Chul Lee, Young Ho Jeon, Chaejoon Cheong, Hye Yeon Kim

Research output: Contribution to journal › Article › peer-review

1 Citation (Scopus)

Abstract

OmpA-like domain proteins bind to peptidoglycan by interacting with the D-amino acid moiety of meso-diaminopimelate in peptidoglycan, but it is still not clear how this domain recognizes the D-amino region of peptidoglycan. To study their D-stereoisomer preference, we solved the crystal structures of the OmpA-like domains of Acinetobacter baumannii peptidoglycan-associated lipoprotein (AbPal) in complex with D- or L-diaminopimelate. Our results reveal that these domains can bind both enantiomers of diaminopimelate with a greater affinity for D-diaminopimelate. The crystal structures of wild-type AbPal in complex with meso-diaminopimelate and mutant AbPal in complete with the LL-diaminopimelate ligand suggests that the Tyr85 residue of AbPal is an important determinant for this D-amino acid moiety preference. Our findings provide a basis for the development of antibacterial agents that inhibit interactions between PGN and OmpA-like domains and disrupt the stability of cell walls of gram-negative bacteria.

Original language	English
Pages (from-to)	110-115
Number of pages	6
Journal	Process Biochemistry
Volume	55
DOIs	https://doi.org/10.1016/j.procbio.2017.01.009
Publication status	Published - 2017 Apr 1

Bibliographical note

Funding Information:
We thank the beamline staff at the Photon Factory (Tsukuba, Japan) and PAL (Pohang, South Korea) for assistance with the X-ray data collection. This study made use of macromolecular X-ray, Mosquito and isothermal titration calorimetry (ITC) at the Korea Basic Science Institute. This work was supported by the Korea Basic Science Institute grant (C36960 and T37412), the National Research Council of Science & Technology (NST) grant (CRC-16-01-KRICT), and the Korea University grant. This research was also supported by Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education (No. 2016R1A6A3A11931199 and a grant of the Korean Health Technology R&D Project, Ministry of Health & Welfare (No. HI14C2726)

Publisher Copyright:
© 2017 Elsevier Ltd

Keywords

AbPal
Diaminopimelate
OmpA-like domain
Peptidoglycan
Peptidoglycan-associated lipoprotein

ASJC Scopus subject areas

Bioengineering
Biochemistry
Applied Microbiology and Biotechnology

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10.1016/j.procbio.2017.01.009

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title = "D-Stereoisomer preference of the OmpA-like domain of Pal in peptidoglycan of Acinetobacter baumannii",

abstract = "OmpA-like domain proteins bind to peptidoglycan by interacting with the D-amino acid moiety of meso-diaminopimelate in peptidoglycan, but it is still not clear how this domain recognizes the D-amino region of peptidoglycan. To study their D-stereoisomer preference, we solved the crystal structures of the OmpA-like domains of Acinetobacter baumannii peptidoglycan-associated lipoprotein (AbPal) in complex with D- or L-diaminopimelate. Our results reveal that these domains can bind both enantiomers of diaminopimelate with a greater affinity for D-diaminopimelate. The crystal structures of wild-type AbPal in complex with meso-diaminopimelate and mutant AbPal in complete with the LL-diaminopimelate ligand suggests that the Tyr85 residue of AbPal is an important determinant for this D-amino acid moiety preference. Our findings provide a basis for the development of antibacterial agents that inhibit interactions between PGN and OmpA-like domains and disrupt the stability of cell walls of gram-negative bacteria.",

keywords = "AbPal, Diaminopimelate, OmpA-like domain, Peptidoglycan, Peptidoglycan-associated lipoprotein",

author = "Yeo, {Kwon Joo} and Lee, {Woo Cheol} and Saeyoung Lee and Eunha Hwang and Park, {Jeong Soon} and Choi, {In Geol} and Kim, {Seung Il} and Lee, {Je Chul} and Jeon, {Young Ho} and Chaejoon Cheong and Kim, {Hye Yeon}",

note = "Funding Information: We thank the beamline staff at the Photon Factory (Tsukuba, Japan) and PAL (Pohang, South Korea) for assistance with the X-ray data collection. This study made use of macromolecular X-ray, Mosquito and isothermal titration calorimetry (ITC) at the Korea Basic Science Institute. This work was supported by the Korea Basic Science Institute grant (C36960 and T37412), the National Research Council of Science & Technology (NST) grant (CRC-16-01-KRICT), and the Korea University grant. This research was also supported by Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education (No. 2016R1A6A3A11931199 and a grant of the Korean Health Technology R&D Project, Ministry of Health & Welfare (No. HI14C2726) Publisher Copyright: {\textcopyright} 2017 Elsevier Ltd",

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month = apr,

day = "1",

doi = "10.1016/j.procbio.2017.01.009",

language = "English",

volume = "55",

pages = "110--115",

journal = "Process Biochemistry",

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T1 - D-Stereoisomer preference of the OmpA-like domain of Pal in peptidoglycan of Acinetobacter baumannii

AU - Yeo, Kwon Joo

AU - Lee, Woo Cheol

AU - Lee, Saeyoung

AU - Hwang, Eunha

AU - Park, Jeong Soon

AU - Choi, In Geol

AU - Kim, Seung Il

AU - Lee, Je Chul

AU - Jeon, Young Ho

AU - Cheong, Chaejoon

AU - Kim, Hye Yeon

N1 - Funding Information: We thank the beamline staff at the Photon Factory (Tsukuba, Japan) and PAL (Pohang, South Korea) for assistance with the X-ray data collection. This study made use of macromolecular X-ray, Mosquito and isothermal titration calorimetry (ITC) at the Korea Basic Science Institute. This work was supported by the Korea Basic Science Institute grant (C36960 and T37412), the National Research Council of Science & Technology (NST) grant (CRC-16-01-KRICT), and the Korea University grant. This research was also supported by Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education (No. 2016R1A6A3A11931199 and a grant of the Korean Health Technology R&D Project, Ministry of Health & Welfare (No. HI14C2726) Publisher Copyright: © 2017 Elsevier Ltd

PY - 2017/4/1

Y1 - 2017/4/1

N2 - OmpA-like domain proteins bind to peptidoglycan by interacting with the D-amino acid moiety of meso-diaminopimelate in peptidoglycan, but it is still not clear how this domain recognizes the D-amino region of peptidoglycan. To study their D-stereoisomer preference, we solved the crystal structures of the OmpA-like domains of Acinetobacter baumannii peptidoglycan-associated lipoprotein (AbPal) in complex with D- or L-diaminopimelate. Our results reveal that these domains can bind both enantiomers of diaminopimelate with a greater affinity for D-diaminopimelate. The crystal structures of wild-type AbPal in complex with meso-diaminopimelate and mutant AbPal in complete with the LL-diaminopimelate ligand suggests that the Tyr85 residue of AbPal is an important determinant for this D-amino acid moiety preference. Our findings provide a basis for the development of antibacterial agents that inhibit interactions between PGN and OmpA-like domains and disrupt the stability of cell walls of gram-negative bacteria.

AB - OmpA-like domain proteins bind to peptidoglycan by interacting with the D-amino acid moiety of meso-diaminopimelate in peptidoglycan, but it is still not clear how this domain recognizes the D-amino region of peptidoglycan. To study their D-stereoisomer preference, we solved the crystal structures of the OmpA-like domains of Acinetobacter baumannii peptidoglycan-associated lipoprotein (AbPal) in complex with D- or L-diaminopimelate. Our results reveal that these domains can bind both enantiomers of diaminopimelate with a greater affinity for D-diaminopimelate. The crystal structures of wild-type AbPal in complex with meso-diaminopimelate and mutant AbPal in complete with the LL-diaminopimelate ligand suggests that the Tyr85 residue of AbPal is an important determinant for this D-amino acid moiety preference. Our findings provide a basis for the development of antibacterial agents that inhibit interactions between PGN and OmpA-like domains and disrupt the stability of cell walls of gram-negative bacteria.

KW - AbPal

KW - Diaminopimelate

KW - OmpA-like domain

KW - Peptidoglycan

KW - Peptidoglycan-associated lipoprotein

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U2 - 10.1016/j.procbio.2017.01.009

DO - 10.1016/j.procbio.2017.01.009

M3 - Article

AN - SCOPUS:85010901095

SN - 1359-5113

VL - 55

SP - 110

EP - 115

JO - Process Biochemistry

JF - Process Biochemistry

ER -

D-Stereoisomer preference of the OmpA-like domain of Pal in peptidoglycan of Acinetobacter baumannii

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

Access to Document

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