1obr
From Proteopedia
(New page: 200px<br /><applet load="1obr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1obr, resolution 2.3Å" /> '''CARBOXYPEPTIDASE T'''...) |
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| - | [[Image:1obr.gif|left|200px]]<br /><applet load="1obr" size=" | + | [[Image:1obr.gif|left|200px]]<br /><applet load="1obr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1obr, resolution 2.3Å" /> | caption="1obr, resolution 2.3Å" /> | ||
'''CARBOXYPEPTIDASE T'''<br /> | '''CARBOXYPEPTIDASE T'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of carboxypeptidase T from Thermoactinomyces | + | The crystal structure of carboxypeptidase T from Thermoactinomyces vulgaris has been determined at 0.235-nm resolution by X-ray diffraction. Carboxypeptidase T is a remote homologue of mammalian Zn-carboxypeptidases. In spite of the low degree of amino acid sequence identity, the three-dimensional structure of carboxypeptidase T is very similar to that of pancreatic carboxypeptidases A and B. The core of the protein molecule is formed by an eight-stranded mixed beta sheet. The active site is located at the C-edge of the central (parallel) part of the beta sheet. The structural organization of the active centre appears to be essentially the same in the three carboxypeptidases. Amino acid residues directly involved in catalysis and binding of the C-terminal carboxyl of a substrate are strictly conserved. This suggests that the catalytic mechanism proposed for the pancreatic enzymes is applicable to carboxypeptidase T and to the whole family of Zn-carboxypeptidases. Comparison of the amino acid replacements at the primary specificity pocket of carboxypeptidases A, B and T provides an explanation of the unusual 'A+B' type of specificity of carboxypeptidase T. Four calcium-binding sites localized in the crystal structure of carboxypeptidase T could account for the high thermostability of the protein. |
==About this Structure== | ==About this Structure== | ||
| - | 1OBR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris] with ZN, CA and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Carboxypeptidase_T Carboxypeptidase T], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.18 3.4.17.18] Full crystallographic information is available from [http:// | + | 1OBR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Carboxypeptidase_T Carboxypeptidase T], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.18 3.4.17.18] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OBR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:15:50 2008'' |
Revision as of 12:15, 21 February 2008
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CARBOXYPEPTIDASE T
Overview
The crystal structure of carboxypeptidase T from Thermoactinomyces vulgaris has been determined at 0.235-nm resolution by X-ray diffraction. Carboxypeptidase T is a remote homologue of mammalian Zn-carboxypeptidases. In spite of the low degree of amino acid sequence identity, the three-dimensional structure of carboxypeptidase T is very similar to that of pancreatic carboxypeptidases A and B. The core of the protein molecule is formed by an eight-stranded mixed beta sheet. The active site is located at the C-edge of the central (parallel) part of the beta sheet. The structural organization of the active centre appears to be essentially the same in the three carboxypeptidases. Amino acid residues directly involved in catalysis and binding of the C-terminal carboxyl of a substrate are strictly conserved. This suggests that the catalytic mechanism proposed for the pancreatic enzymes is applicable to carboxypeptidase T and to the whole family of Zn-carboxypeptidases. Comparison of the amino acid replacements at the primary specificity pocket of carboxypeptidases A, B and T provides an explanation of the unusual 'A+B' type of specificity of carboxypeptidase T. Four calcium-binding sites localized in the crystal structure of carboxypeptidase T could account for the high thermostability of the protein.
About this Structure
1OBR is a Single protein structure of sequence from Thermoactinomyces vulgaris with , and as ligands. Active as Carboxypeptidase T, with EC number 3.4.17.18 Full crystallographic information is available from OCA.
Reference
Crystal structure of carboxypeptidase T from Thermoactinomyces vulgaris., Teplyakov A, Polyakov K, Obmolova G, Strokopytov B, Kuranova I, Osterman A, Grishin N, Smulevitch S, Zagnitko O, Galperina O, et al., Eur J Biochem. 1992 Sep 1;208(2):281-8. PMID:1521526
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