1zq8

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{{STRUCTURE_1zq8| PDB=1zq8 | SCENE= }}
{{STRUCTURE_1zq8| PDB=1zq8 | SCENE= }}
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'''Crystal Structure of N-acetyl-L-ornithine transcarbamylase complexed with carbamoyl phosphate and N-acetyl-L-norvaline'''
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===Crystal Structure of N-acetyl-L-ornithine transcarbamylase complexed with carbamoyl phosphate and N-acetyl-L-norvaline===
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==Overview==
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N-acetyl-L-ornithine transcarbamoylase (AOTCase) is a new member of the transcarbamoylase superfamily that is essential for arginine biosynthesis in several eubacteria. We report here crystal structures of the binary complexes of AOTCase with its substrates, carbamoyl phosphate (CP) or N-acetyl-L-ornithine (AORN), and the ternary complex with CP and N-acetyl-L-norvaline. Comparison of these structures demonstrates that the substrate-binding mechanism of this novel transcarbamoylase is different from those of aspartate and ornithine transcarbamoylases, both of which show ordered substrate binding with large domain movements. CP and AORN bind to AOTCase independently, and the main conformational change upon substrate binding is ordering of the 80's loop, with a small domain closure around the active site and little movement of the 240's loop. The structures of the complexes provide insight into the mode of substrate binding and the mechanism of the transcarbamoylation reaction.
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{{ABSTRACT_PUBMED_16741992}}
==About this Structure==
==About this Structure==
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[[Category: Yu, X.]]
[[Category: Yu, X.]]
[[Category: Alpha/beta two-domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:56:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:39:08 2008''

Revision as of 21:39, 28 July 2008

Template:STRUCTURE 1zq8

Crystal Structure of N-acetyl-L-ornithine transcarbamylase complexed with carbamoyl phosphate and N-acetyl-L-norvaline

Template:ABSTRACT PUBMED 16741992

About this Structure

1ZQ8 is a Single protein structure of sequence from Xanthomonas campestris. Full crystallographic information is available from OCA.

Reference

Structures of N-acetylornithine transcarbamoylase from Xanthomonas campestris complexed with substrates and substrate analogs imply mechanisms for substrate binding and catalysis., Shi D, Yu X, Roth L, Morizono H, Tuchman M, Allewell NM, Proteins. 2006 Aug 1;64(2):532-42. PMID:16741992

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