3ci4: Difference between revisions

From Proteopedia
Jump to navigationJump to search
Newer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
New page: left|200px <!-- The line below this paragraph, containing "STRUCTURE_3ci4", creates the "Structure Box" on the page. You may change the PDB parameter (which sets the PD...
 
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
Line 1: Line 1:
[[Image:3ci4.jpg|left|200px]]
{{Seed}}
[[Image:3ci4.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_3ci4|  PDB=3ci4  |  SCENE=  }}  
{{STRUCTURE_3ci4|  PDB=3ci4  |  SCENE=  }}  


'''Structure of the PduO-type ATP:co(I)rrinoid adenosyltransferase from Lactobacillus reuteri complexed with four-coordinate cob(II)inamide and ATP'''
===Structure of the PduO-type ATP:co(I)rrinoid adenosyltransferase from Lactobacillus reuteri complexed with four-coordinate cob(II)inamide and ATP===




==Overview==
<!--  
ATP:cob(I)alamin adenosyltransferases (ACAs) catalyze the transfer of the 5'-deoxyadenosyl moiety from ATP to the upper axial ligand position of cobalamin in the synthesis of coenzyme B 12. For the ACA-catalyzed reaction to proceed, cob(II)alamin must be reduced to cob(I)alamin in the enzyme active site. This reduction is facilitated through the generation of a four-coordinate cob(II)alamin intermediate on the enzyme. We have determined the high-resolution crystal structure of a human-type ACA from Lactobacillus reuteri with a four-coordinate cob(II)alamin bound in the enzyme active site and with the product, adenosylcobalamin, partially occupied in the active site. The assembled structures represent snapshots of the steps in the ACA-catalyzed formation of the cobalt-carbon bond of coenzyme B 12. The structures define the corrinoid binding site and provide visual evidence for a base-off, four-coordinate cob(II)alamin intermediate. The complete structural description of ACA-mediated catalysis reveals the molecular features of four-coordinate cob(II)alamin stabilization and provides additional insights into the molecular basis for dysfunction in human patients suffering from methylmalonic aciduria.
The line below this paragraph, {{ABSTRACT_PUBMED_18452306}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 18452306 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_18452306}}


==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Atp binding]]
[[Category: Atp binding]]
[[Category: Corrin binding]]
[[Category: Corrin binding]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 28 09:22:23 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:08:54 2008''

Revision as of 05:08, 29 July 2008

File:3ci4.png

Template:STRUCTURE 3ci4

Structure of the PduO-type ATP:co(I)rrinoid adenosyltransferase from Lactobacillus reuteri complexed with four-coordinate cob(II)inamide and ATP

Template:ABSTRACT PUBMED 18452306

About this Structure

3CI4 is a Single protein structure of sequence from Lactobacillus reuteri. Full crystallographic information is available from OCA.

Reference

Structural characterization of a human-type corrinoid adenosyltransferase confirms that coenzyme B12 is synthesized through a four-coordinate intermediate., St Maurice M, Mera P, Park K, Brunold TC, Escalante-Semerena JC, Rayment I, Biochemistry. 2008 May 27;47(21):5755-66. Epub 2008 May 2. PMID:18452306

Page seeded by OCA on Tue Jul 29 08:08:54 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=3ci4&oldid=734035"