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 journalArticle

1 Citation (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 B 12. 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 languageEnglish
Pages (from-to)417-421
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume408
Issue number3
DOIs
Publication statusPublished - 2011 May 13

Fingerprint

Bacillus cereus
Adenosine Triphosphate
Crystal structure
Vitamin B 12
Catalytic Domain
Molecules
Hydrogen Bonding
Hydrogen bonds
cob(I)alamin adenosyltransferase
Substrates
Enzymes

Keywords

  • Adenosylcobalamin
  • Adenosyltransferase
  • Cobalamin
  • MgATP
  • PduO

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology

Cite this

Crystal structure of PduO-Type ATP : Cob(I)alamin adenosyltransferase from Bacillus cereus in a complex with ATP. / Park, Ae Kyung; Chi, Young Min; Moon, Jin Ho.

In: Biochemical and Biophysical Research Communications, Vol. 408, No. 3, 13.05.2011, p. 417-421.

Research output: Contribution to journalArticle

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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 B 12. 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 B 12. 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.

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