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| - | [[Image:1b7b.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1b7b| PDB=1b7b | SCENE= }} | | {{STRUCTURE_1b7b| PDB=1b7b | SCENE= }} |
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| - | '''Carbamate kinase from Enterococcus faecalis'''
| + | ===Carbamate kinase from Enterococcus faecalis=== |
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| - | ==Overview==
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| - | The enzymes carbamoyl phosphate synthetase (CPS) and carbamate kinase (CK) make carbamoyl phosphate in the same way: by ATP-phosphorylation of carbamate. The carbamate used by CK is made chemically, whereas CPS itself synthesizes its own carbamate in a process involving the phosphorylation of bicarbonate. Bicarbonate and carbamate are analogs and the phosphorylations are carried out by homologous 40 kDa regions of the 120 kDa CPS polypeptide. CK can also phosphorylate bicarbonate and is a homodimer of a 33 kDa subunit that was believed to resemble the 40 kDa regions of CPS. Such belief is disproven now by the CK structure reported here. The structure does not conform to the biotin carboxylase fold found in the 40 kDa regions of CPS, and presents a new type of fold possibly shared by homologous acylphosphate-making enzymes. A molecular 16-stranded open beta-sheet surrounded by alpha-helices is the hallmark of the CK dimer. Each subunit also contains two smaller sheets and a large crevice found at the location expected for the active center. Intersubunit interactions are very large and involve a central hydrophobic patch and more hydrophilic peripheral contacts. The crevice holds a sulfate that may occupy the site of an ATP phosphate, and is lined by conserved residues. Site-directed mutations tested at two of these residues inactivate the enzyme. These findings support active site location in the crevice. The orientation of the crevices in the dimer precludes their physical cooperation in the catalytic process. Such cooperation is not needed in the CK reaction but is a requirement of the mechanism of CPSs. | + | The line below this paragraph, {{ABSTRACT_PUBMED_10211841}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10211841 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10211841}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Open alpha/beta sheet]] | | [[Category: Open alpha/beta sheet]] |
| | [[Category: Phosphotransferase]] | | [[Category: Phosphotransferase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:09:48 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:26:35 2008'' |
Revision as of 15:26, 30 June 2008
Template:STRUCTURE 1b7b
Carbamate kinase from Enterococcus faecalis
Template:ABSTRACT PUBMED 10211841
About this Structure
1B7B is a Single protein structure of sequence from Enterococcus faecium. Full crystallographic information is available from OCA.
Reference
Carbamate kinase: New structural machinery for making carbamoyl phosphate, the common precursor of pyrimidines and arginine., Marina A, Alzari PM, Bravo J, Uriarte M, Barcelona B, Fita I, Rubio V, Protein Sci. 1999 Apr;8(4):934-40. PMID:10211841
Page seeded by OCA on Mon Jun 30 18:26:35 2008
