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| | {{STRUCTURE_1pv9| PDB=1pv9 | SCENE= }} | | {{STRUCTURE_1pv9| PDB=1pv9 | SCENE= }} |
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| - | '''Prolidase from Pyrococcus furiosus'''
| + | ===Prolidase from Pyrococcus furiosus=== |
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| - | ==Overview==
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| - | The structure of prolidase from the hyperthermophilic archaeon Pyrococcus furiosus (Pfprol) has been solved and refined at 2.0 A resolution. This is the first structure of a prolidase, i.e., a peptidase specific for dipeptides having proline as the second residue. The asymmetric unit of the crystals contains a homodimer of the enzyme. Each of the two protein subunits has two domains. The C-terminal domain includes the catalytic site, which is centered on a dinuclear metal cluster. In the as-isolated form of Pfprol, the active-site metal atoms are Co(II) [Ghosh, M., et al. (1998) J. Bacteriol. 180, 4781-9]. An unexpected finding is that in the crystalline enzyme the active-site metal atoms are Zn(II), presumably as a result of metal exchange during crystallization. Both of the Zn(II) atoms are five-coordinate. The ligands include a bridging water molecule or hydroxide ion, which is likely to act as a nucleophile in the catalytic reaction. The two-domain polypeptide fold of Pfprol is similar to the folds of two functionally related enzymes, aminopeptidase P (APPro) and creatinase. In addition, the catalytic C-terminal domain of Pfprol has a polypeptide fold resembling that of the sole domain of a fourth enzyme, methionine aminopeptidase (MetAP). The active sites of APPro and MetAP, like that of Pfprol, include a dinuclear metal center. The metal ligands in the three enzymes are homologous. Comparisons with the molecular structures of APPro and MetAP suggest how Pfprol discriminates against oligopeptides and in favor of Xaa-Pro substrates. The crystal structure of Pfprol was solved by multiple-wavelength anomalous dispersion. The crystals yielded diffraction data of relatively high quality and resolution, despite the fact that one of the two protein subunits in the asymmetric unit was found to be significantly disordered. The final R and R(free) values are 0.24 and 0.28, respectively. | + | The line below this paragraph, {{ABSTRACT_PUBMED_15005612}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15005612 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15005612}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Prolidase]] | | [[Category: Prolidase]] |
| | [[Category: Zinc]] | | [[Category: Zinc]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:31:30 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:31:57 2008'' |
Revision as of 06:32, 28 July 2008
Template:STRUCTURE 1pv9
Prolidase from Pyrococcus furiosus
Template:ABSTRACT PUBMED 15005612
About this Structure
1PV9 is a Single protein structure of sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA.
Reference
Structure of the prolidase from Pyrococcus furiosus., Maher MJ, Ghosh M, Grunden AM, Menon AL, Adams MW, Freeman HC, Guss JM, Biochemistry. 2004 Mar 16;43(10):2771-83. PMID:15005612
Page seeded by OCA on Mon Jul 28 09:31:57 2008
