2otc: Difference between revisions
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[[Image:2otc.gif|left|200px]] | [[Image:2otc.gif|left|200px]] | ||
'''ORNITHINE TRANSCARBAMOYLASE COMPLEXED WITH N-(PHOSPHONACETYL)-L-ORNITHINE''' | {{Structure | ||
|PDB= 2otc |SIZE=350|CAPTION= <scene name='initialview01'>2otc</scene>, resolution 2.8Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=PAO:N-(PHOSPHONOACETYL)-L-ORNITHINE'>PAO</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= ARGI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''ORNITHINE TRANSCARBAMOYLASE COMPLEXED WITH N-(PHOSPHONACETYL)-L-ORNITHINE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2OTC is a [ | 2OTC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OTC OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9275160 9275160] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Ornithine carbamoyltransferase]] | [[Category: Ornithine carbamoyltransferase]] | ||
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[[Category: urea cycle]] | [[Category: urea cycle]] | ||
''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 18:04:12 2008'' | ||
Revision as of 19:04, 20 March 2008
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| , resolution 2.8Å | |||||||
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| Ligands: | |||||||
| Gene: | ARGI (Escherichia coli) | ||||||
| Activity: | Ornithine carbamoyltransferase, with EC number 2.1.3.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ORNITHINE TRANSCARBAMOYLASE COMPLEXED WITH N-(PHOSPHONACETYL)-L-ORNITHINE
OverviewOverview
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. & 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.
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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