7req: Difference between revisions

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[[Image:7req.gif|left|200px]]
{{Seed}}
[[Image:7req.png|left|200px]]


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{{STRUCTURE_7req|  PDB=7req  |  SCENE=  }}  
{{STRUCTURE_7req|  PDB=7req  |  SCENE=  }}  


'''METHYLMALONYL-COA MUTASE, 2-CARBOXYPROPYL-COA INHIBITOR COMPLEX'''
===METHYLMALONYL-COA MUTASE, 2-CARBOXYPROPYL-COA INHIBITOR COMPLEX===




==Overview==
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X-ray crystal structures of methylmalonyl-CoA mutase in complexes with substrate methylmalonyl-CoA and inhibitors 2-carboxypropyl-CoA and 3-carboxypropyl-CoA (substrate and product analogues) show that the enzyme-substrate interactions change little during the course of the rearrangement reaction, in contrast to the large conformational change on substrate binding. The substrate complex shows a 5'-deoxyadenine molecule in the active site, bound weakly and not attached to the cobalt atom of coenzyme B12, rotated and shifted from its position in the substrate-free adenosylcobalamin complex. The position of Tyralpha89 close to the substrate explains the stereochemical selectivity of the enzyme for (2R)-methylmalonyl-CoA.
The line below this paragraph, {{ABSTRACT_PUBMED_10387043}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 10387043 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10387043}}


==About this Structure==
==About this Structure==
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[[Category: Isomerase]]
[[Category: Isomerase]]
[[Category: Mutase]]
[[Category: Mutase]]
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