1fvo: Difference between revisions

Revision as of 04:00, 1 July 2008

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File:1fvo.png

Template:STRUCTURE 1fvo

CRYSTAL STRUCTURE OF HUMAN ORNITHINE TRANSCARBAMYLASE COMPLEXED WITH CARBAMOYL PHOSPHATECRYSTAL STRUCTURE OF HUMAN ORNITHINE TRANSCARBAMYLASE COMPLEXED WITH CARBAMOYL PHOSPHATE

Template:ABSTRACT PUBMED 11237854

About this StructureAbout this Structure

1FVO is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Human ornithine transcarbamylase: crystallographic insights into substrate recognition and conformational changes., Shi D, Morizono H, Yu X, Tong L, Allewell NM, Tuchman M, Biochem J. 2001 Mar 15;354(Pt 3):501-9. PMID:11237854

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''CRYSTAL STRUCTURE OF HUMAN ORNITHINE TRANSCARBAMYLASE COMPLEXED WITH CARBAMOYL PHOSPHATE'''
+===CRYSTAL STRUCTURE OF HUMAN ORNITHINE TRANSCARBAMYLASE COMPLEXED WITH CARBAMOYL PHOSPHATE===
-==Overview==
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-Two crystal structures of human ornithine transcarbamylase (OTCase) complexed with the substrate carbamoyl phosphate (CP) have been solved. One structure, whose crystals were prepared by substituting N-phosphonacetyl-L-ornithine (PALO) liganded crystals with CP, has been refined at 2.4 A (1 A=0.1 nm) resolution to a crystallographic R factor of 18.4%. The second structure, whose crystals were prepared by co-crystallization with CP, has been refined at 2.6 A resolution to a crystallographic R factor of 20.2%. These structures provide important new insights into substrate recognition and ligand-induced conformational changes. Comparison of these structures with the structures of OTCase complexed with the bisubstrate analogue PALO or CP and L-norvaline reveals that binding of the first substrate, CP, induces a global conformational change involving relative domain movement, whereas the binding of the second substrate brings the flexible SMG loop, which is equivalent to the 240s loop in aspartate transcarbamylase, into the active site. The model reveals structural features that define the substrate specificity of the enzyme and that regulate the order of binding and release of products.
+The line below this paragraph, {{ABSTRACT_PUBMED_11237854}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11237854 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_11237854}}
 ==About this Structure==
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 [[Category: Alpha/beta topology]]
 [[Category: Two domain]]
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