2vid: Difference between revisions

Revision as of 16:26, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2vid.png

Template:STRUCTURE 2vid

SERINE PROTEASE SPLB FROM STAPHYLOCOCCUS AUREUS AT 1.8A RESOLUTIONSERINE PROTEASE SPLB FROM STAPHYLOCOCCUS AUREUS AT 1.8A RESOLUTION

Template:ABSTRACT PUBMED 18448121

About this StructureAbout this Structure

2VID is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

ReferenceReference

Enzymatic activity of the Staphylococcus aureus SplB serine protease is induced by substrates containing the sequence Trp-Glu-Leu-Gln., Dubin G, Stec-Niemczyk J, Kisielewska M, Pustelny K, Popowicz GM, Bista M, Kantyka T, Boulware KT, Stennicke HR, Czarna A, Phopaisarn M, Daugherty PS, Thogersen IB, Enghild JJ, Thornberry N, Dubin A, Potempa J, J Mol Biol. 2008 May 30;379(2):343-56. Epub 2008 Apr 3. PMID:18448121

Functional and structural characterization of Spl proteases from Staphylococcus aureus., Popowicz GM, Dubin G, Stec-Niemczyk J, Czarny A, Dubin A, Potempa J, Holak TA, J Mol Biol. 2006 Apr 21;358(1):270-9. Epub 2006 Feb 13. PMID:16516230

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OCA

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-[[Image:2vid.jpg|left|200px]]
+{{Seed}}
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 {{STRUCTURE_2vid|  PDB=2vid  |  SCENE=  }}
-'''SERINE PROTEASE SPLB FROM STAPHYLOCOCCUS AUREUS AT 1.8A RESOLUTION'''
+===SERINE PROTEASE SPLB FROM STAPHYLOCOCCUS AUREUS AT 1.8A RESOLUTION===
-==Overview==
+<!--
-Proteases are of significant importance for the virulence of Staphylococcus aureus. Nevertheless, their subset, the serine protease-like proteins, remains poorly characterized. Here presented is an investigation of SplB protease catalytic activity revealing that the enzyme possesses exquisite specificity and only cleaves efficiently after the sequence Trp-Glu-Leu-Gln. To understand the molecular basis for such selectivity, we solved the three-dimensional structure of SplB to 1.8 A. Modeling of substrate binding to the protease demonstrated that selectivity relies in part on a canonical specificity pockets-based mechanism. Significantly, the conformation of residues that ordinarily form the oxyanion hole, an essential structural element of the catalytic machinery of serine proteases, is not canonical in the SplB structure. We postulate that within SplB, the oxyanion hole is only formed upon docking of a substrate containing the consensus sequence motif. It is suggested that this unusual activation mechanism is used in parallel with classical determinants to further limit enzyme specificity. Finally, to guide future development, we attempt to point at likely physiological substrates and thus the role of SplB in staphylococcal physiology.
+The line below this paragraph, {{ABSTRACT_PUBMED_18448121}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18448121 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18448121}}
 ==About this Structure==
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 ==Reference==
 Enzymatic activity of the Staphylococcus aureus SplB serine protease is induced by substrates containing the sequence Trp-Glu-Leu-Gln., Dubin G, Stec-Niemczyk J, Kisielewska M, Pustelny K, Popowicz GM, Bista M, Kantyka T, Boulware KT, Stennicke HR, Czarna A, Phopaisarn M, Daugherty PS, Thogersen IB, Enghild JJ, Thornberry N, Dubin A, Potempa J, J Mol Biol. 2008 May 30;379(2):343-56. Epub 2008 Apr 3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18448121 18448121]
+Functional and structural characterization of Spl proteases from Staphylococcus aureus., Popowicz GM, Dubin G, Stec-Niemczyk J, Czarny A, Dubin A, Potempa J, Holak TA, J Mol Biol. 2006 Apr 21;358(1):270-9. Epub 2006 Feb 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16516230 16516230]
 [[Category: Single protein]]
 [[Category: Staphylococcus aureus]]
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 [[Category: Serine protease]]
 [[Category: Staphylococcus aureus]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 14 11:25:42 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:26:20 2008''