2otc: Difference between revisions

Revision as of 23:10, 27 July 2008

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File:2otc.png

Template:STRUCTURE 2otc

ORNITHINE TRANSCARBAMOYLASE COMPLEXED WITH N-(PHOSPHONACETYL)-L-ORNITHINEORNITHINE TRANSCARBAMOYLASE COMPLEXED WITH N-(PHOSPHONACETYL)-L-ORNITHINE

Template:ABSTRACT PUBMED 9275160

About this StructureAbout this Structure

2OTC is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Substrate-induced conformational change in a trimeric ornithine transcarbamoylase., Ha Y, McCann MT, Tuchman M, Allewell NM, Proc Natl Acad Sci U S A. 1997 Sep 2;94(18):9550-5. PMID:9275160

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-[[Image:2otc.gif|left|200px]]
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 {{STRUCTURE_2otc|  PDB=2otc  |  SCENE=  }}
-'''ORNITHINE TRANSCARBAMOYLASE COMPLEXED WITH N-(PHOSPHONACETYL)-L-ORNITHINE'''
+===ORNITHINE TRANSCARBAMOYLASE COMPLEXED WITH N-(PHOSPHONACETYL)-L-ORNITHINE===
-==Overview==
+<!--
-The crystal structure of Escherichia coli ornithine transcarbamoylase (OTCase, EC 2.1.3.3) complexed with the bisubstrate analog N-(phosphonacetyl)-L-ornithine (PALO) has been determined at 2.8-A resolution. This research on the structure of a transcarbamoylase catalytic trimer with a substrate analog bound provides new insights into the linkages between substrate binding, protein-protein interactions, and conformational change. The structure was solved by molecular replacement with the Pseudomonas aeruginosa catabolic OTCase catalytic trimer (Villeret, V., Tricot, C., Stalon, V. &amp; Dideberg, O. (1995) Proc. Natl. Acad. Sci. USA 92, 10762-10766; Protein Data Bank reference pdb 1otc) as the model and refined to a crystallographic R value of 21.3%. Each polypeptide chain folds into two domains, a carbamoyl phosphate binding domain and an L-ornithine binding domain. The bound inhibitor interacts with the side chains and/or backbone atoms of Lys-53, Ser-55, Thr-56, Arg-57, Thr-58, Arg-106, His-133, Asn-167, Asp-231, Met-236, Leu-274, Arg-319 as well as Gln-82 and Lys-86 from an adjacent chain. Comparison with the unligated P. aeruginosa catabolic OTCase structure indicates that binding of the substrate analog results in closure of the two domains of each chain. As in E. coli aspartate transcarbamoylase, the 240s loop undergoes the largest conformational change upon substrate binding. The clinical implications for human OTCase deficiency are discussed.
+The line below this paragraph, {{ABSTRACT_PUBMED_9275160}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_9275160}}
 ==About this Structure==
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 [[Category: Transferase]]
 [[Category: Urea cycle]]
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