1s2k
From Proteopedia
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| - | [[Image:1s2k.jpg|left|200px]] | + | [[Image:1s2k.jpg|left|200px]] |
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| - | '''Structure of SCP-B a member of the Eqolisin family of Peptidases in a complex with a Tripeptide Ala-Ile-His''' | + | {{Structure |
| + | |PDB= 1s2k |SIZE=350|CAPTION= <scene name='initialview01'>1s2k</scene>, resolution 2.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=TYR:TYROSINE'>TYR</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Scytalidopepsin_B Scytalidopepsin B], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.32 3.4.23.32] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Structure of SCP-B a member of the Eqolisin family of Peptidases in a complex with a Tripeptide Ala-Ile-His''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1S2K is a [ | + | 1S2K is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Scytalidium_lignicola Scytalidium lignicola]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S2K OCA]. |
==Reference== | ==Reference== | ||
| - | The molecular structure and catalytic mechanism of a novel carboxyl peptidase from Scytalidium lignicolum., Fujinaga M, Cherney MM, Oyama H, Oda K, James MN, Proc Natl Acad Sci U S A. 2004 Mar 9;101(10):3364-9. Epub 2004 Mar 1. PMID:[http:// | + | The molecular structure and catalytic mechanism of a novel carboxyl peptidase from Scytalidium lignicolum., Fujinaga M, Cherney MM, Oyama H, Oda K, James MN, Proc Natl Acad Sci U S A. 2004 Mar 9;101(10):3364-9. Epub 2004 Mar 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14993599 14993599] |
[[Category: Scytalidium lignicola]] | [[Category: Scytalidium lignicola]] | ||
[[Category: Scytalidopepsin B]] | [[Category: Scytalidopepsin B]] | ||
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[[Category: TYR]] | [[Category: TYR]] | ||
[[Category: beta sandwich]] | [[Category: beta sandwich]] | ||
| - | [[Category: complex with ala-ile- | + | [[Category: complex with ala-ile-hi]] |
[[Category: eqolisin family]] | [[Category: eqolisin family]] | ||
[[Category: pepstatin insensitive carboxyl peptidase]] | [[Category: pepstatin insensitive carboxyl peptidase]] | ||
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[[Category: proteinase]] | [[Category: proteinase]] | ||
| - | ''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 13:59:36 2008'' |
Revision as of 11:59, 20 March 2008
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| , resolution 2.0Å | |||||||
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| Ligands: | |||||||
| Activity: | Scytalidopepsin B, with EC number 3.4.23.32 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of SCP-B a member of the Eqolisin family of Peptidases in a complex with a Tripeptide Ala-Ile-His
Overview
The molecular structure of the pepstatin-insensitive carboxyl peptidase from Scytalidium lignicolum, formerly known as scytalidopepsin B, was solved by multiple isomorphous replacement phasing methods and refined to an R factor of 0.230 (R(free) = 0.246) at 2.1-A resolution. In addition to the structure of the unbound peptidase, the structure of a product complex of cleaved angiotensin II bound in the active site of the enzyme was also determined. We propose the name scytalidocarboxyl peptidase B (SCP-B) for this enzyme. On the basis of conserved, catalytic residues identified at the active site, we suggest the name Eqolisin for the enzyme family. The previously uninvestigated SCP-B fold is that of a beta-sandwich; each sheet has seven antiparallel strands. A tripeptide product, Ala-Ile-His, bound in the active site of SCP-B has allowed for identification of the catalytic residues and the residues in subsites S1, S2, and S3, which are important for substrate binding. The most likely hydrolytic mechanism involves nucleophilic attack of a general base (Glu-136)-activated water (OH(-)) on the si-face of the scissile peptide carbonylcarbon atom to form a tetrahedral intermediate. Electrophilic assistance and oxyanion stabilization is provided by the side-chain amide of Gln-53. Protonation of the leaving-group nitrogen is accomplished by the general acid function of the protonated carboxyl group of Glu-136.
About this Structure
1S2K is a Single protein structure of sequence from Scytalidium lignicola. Full crystallographic information is available from OCA.
Reference
The molecular structure and catalytic mechanism of a novel carboxyl peptidase from Scytalidium lignicolum., Fujinaga M, Cherney MM, Oyama H, Oda K, James MN, Proc Natl Acad Sci U S A. 2004 Mar 9;101(10):3364-9. Epub 2004 Mar 1. PMID:14993599
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