Crystal structure of PduO-Type ATP:Cob(I)alamin adenosyltransferase from Bacillus cereus in a complex with ATP

Ae Kyung Park; Young Min Chi; Jin Ho Moon

doi:10.1016/j.bbrc.2011.04.036

Crystal structure of PduO-Type ATP:Cob(I)alamin adenosyltransferase from Bacillus cereus in a complex with ATP

Ae Kyung Park, Young Min Chi, Jin Ho Moon

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

3 Citations (Scopus)

Abstract

ATP:Cobalamin adenosyltransferases catalyze the transfer a 5′-deoxyadenosyl moiety from ATP to cob(I)alamin in the synthesis of the Co-C bond of coenzyme B₁₂. There are three types of adenosyltransferases, CobA, PduO and EutT. Among these adenosyltransferases, the PduO-type adenosyltransferases is the most widely distributed enzyme. Structural comparisons between apo BcPduO and BcPduO in complex with MgATP revealed that the N-terminal strands of both structures were ordered, which is in contrast with the most previously available PduO-type adenosyltransferase structures. Furthermore, unlike other reported structures, apo BcPduO was bound to additional dioxane molecules causing a side chain conformational change at the Tyr30 residue, which is an important residue that mediates hydrogen bonding with ATP molecules upon binding of cobalamin to the active site. This study provides more structural information into the role of active site residues on substrate binding.

Original language	English
Pages (from-to)	417-421
Number of pages	5
Journal	Biochemical and biophysical research communications
Volume	408
Issue number	3
DOIs	https://doi.org/10.1016/j.bbrc.2011.04.036
Publication status	Published - 2011 May 13

Bibliographical note

Funding Information:
We thank the staff at beamline 6C of Pohang Light Source, South Korea, for assistance during the data collection. This work was supported by a Korea University Grant.

Keywords

Adenosylcobalamin
Adenosyltransferase
Cobalamin
MgATP
PduO

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2011.04.036

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@article{f830aa4450cc4219b3269061d0867ab2,

title = "Crystal structure of PduO-Type ATP:Cob(I)alamin adenosyltransferase from Bacillus cereus in a complex with ATP",

abstract = "ATP:Cobalamin adenosyltransferases catalyze the transfer a 5′-deoxyadenosyl moiety from ATP to cob(I)alamin in the synthesis of the Co-C bond of coenzyme B12. There are three types of adenosyltransferases, CobA, PduO and EutT. Among these adenosyltransferases, the PduO-type adenosyltransferases is the most widely distributed enzyme. Structural comparisons between apo BcPduO and BcPduO in complex with MgATP revealed that the N-terminal strands of both structures were ordered, which is in contrast with the most previously available PduO-type adenosyltransferase structures. Furthermore, unlike other reported structures, apo BcPduO was bound to additional dioxane molecules causing a side chain conformational change at the Tyr30 residue, which is an important residue that mediates hydrogen bonding with ATP molecules upon binding of cobalamin to the active site. This study provides more structural information into the role of active site residues on substrate binding.",

keywords = "Adenosylcobalamin, Adenosyltransferase, Cobalamin, MgATP, PduO",

author = "Park, {Ae Kyung} and Chi, {Young Min} and Moon, {Jin Ho}",

note = "Funding Information: We thank the staff at beamline 6C of Pohang Light Source, South Korea, for assistance during the data collection. This work was supported by a Korea University Grant. ",

year = "2011",

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doi = "10.1016/j.bbrc.2011.04.036",

language = "English",

volume = "408",

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T1 - Crystal structure of PduO-Type ATP:Cob(I)alamin adenosyltransferase from Bacillus cereus in a complex with ATP

AU - Park, Ae Kyung

AU - Chi, Young Min

AU - Moon, Jin Ho

N1 - Funding Information: We thank the staff at beamline 6C of Pohang Light Source, South Korea, for assistance during the data collection. This work was supported by a Korea University Grant.

PY - 2011/5/13

Y1 - 2011/5/13

N2 - ATP:Cobalamin adenosyltransferases catalyze the transfer a 5′-deoxyadenosyl moiety from ATP to cob(I)alamin in the synthesis of the Co-C bond of coenzyme B12. There are three types of adenosyltransferases, CobA, PduO and EutT. Among these adenosyltransferases, the PduO-type adenosyltransferases is the most widely distributed enzyme. Structural comparisons between apo BcPduO and BcPduO in complex with MgATP revealed that the N-terminal strands of both structures were ordered, which is in contrast with the most previously available PduO-type adenosyltransferase structures. Furthermore, unlike other reported structures, apo BcPduO was bound to additional dioxane molecules causing a side chain conformational change at the Tyr30 residue, which is an important residue that mediates hydrogen bonding with ATP molecules upon binding of cobalamin to the active site. This study provides more structural information into the role of active site residues on substrate binding.

AB - ATP:Cobalamin adenosyltransferases catalyze the transfer a 5′-deoxyadenosyl moiety from ATP to cob(I)alamin in the synthesis of the Co-C bond of coenzyme B12. There are three types of adenosyltransferases, CobA, PduO and EutT. Among these adenosyltransferases, the PduO-type adenosyltransferases is the most widely distributed enzyme. Structural comparisons between apo BcPduO and BcPduO in complex with MgATP revealed that the N-terminal strands of both structures were ordered, which is in contrast with the most previously available PduO-type adenosyltransferase structures. Furthermore, unlike other reported structures, apo BcPduO was bound to additional dioxane molecules causing a side chain conformational change at the Tyr30 residue, which is an important residue that mediates hydrogen bonding with ATP molecules upon binding of cobalamin to the active site. This study provides more structural information into the role of active site residues on substrate binding.

KW - Adenosylcobalamin

KW - Adenosyltransferase

KW - Cobalamin

KW - MgATP

KW - PduO

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VL - 408

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IS - 3

ER -

Crystal structure of PduO-Type ATP:Cob(I)alamin adenosyltransferase from Bacillus cereus in a complex with ATP

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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