1ep9
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1ep9.jpg|left|200px]] | + | [[Image:1ep9.jpg|left|200px]] |
| - | + | ||
| - | '''HUMAN ORNITHINE TRANSCARBAMYLASE: CRYSTALLOGRAPHIC INSIGHTS INTO SUBSTRATE RECOGNITION AND CONFORMATIONAL CHANGE''' | + | {{Structure |
| + | |PDB= 1ep9 |SIZE=350|CAPTION= <scene name='initialview01'>1ep9</scene>, resolution 2.4Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CP:PHOSPHORIC ACID MONO(FORMAMIDE)ESTER'>CP</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Ornithine_carbamoyltransferase Ornithine carbamoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.3 2.1.3.3] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HUMAN ORNITHINE TRANSCARBAMYLASE: CRYSTALLOGRAPHIC INSIGHTS INTO SUBSTRATE RECOGNITION AND CONFORMATIONAL CHANGE''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 10: | Line 19: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1EP9 is a [ | + | 1EP9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EP9 OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11237854 11237854] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Ornithine carbamoyltransferase]] | [[Category: Ornithine carbamoyltransferase]] | ||
| Line 25: | Line 34: | ||
[[Category: protein-substrate complex]] | [[Category: protein-substrate complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:58:38 2008'' |
Revision as of 08:58, 20 March 2008
| |||||||
| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Ornithine carbamoyltransferase, with EC number 2.1.3.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN ORNITHINE TRANSCARBAMYLASE: CRYSTALLOGRAPHIC INSIGHTS INTO SUBSTRATE RECOGNITION AND CONFORMATIONAL CHANGE
Contents |
Overview
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.
Disease
Known disease associated with this structure: Ornithine transcarbamylase deficiency OMIM:[300461]
About this Structure
1EP9 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 10:58:38 2008
