1f1s: Difference between revisions

Revision as of 02:20, 1 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:1f1s.png

Template:STRUCTURE 1f1s

CRYSTAL STRUCTURE OF STREPTOCOCCUS AGALACTIAE HYALURONATE LYASE AT 2.1 ANGSTROM RESOLUTION.CRYSTAL STRUCTURE OF STREPTOCOCCUS AGALACTIAE HYALURONATE LYASE AT 2.1 ANGSTROM RESOLUTION.

Template:ABSTRACT PUBMED 11527972

About this StructureAbout this Structure

1F1S is a Single protein structure of sequence from Streptococcus agalactiae. Full crystallographic information is available from OCA.

ReferenceReference

Hyaluronan binding and degradation by Streptococcus agalactiae hyaluronate lyase., Li S, Jedrzejas MJ, J Biol Chem. 2001 Nov 2;276(44):41407-16. Epub 2001 Aug 29. PMID:11527972

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-'''CRYSTAL STRUCTURE OF STREPTOCOCCUS AGALACTIAE HYALURONATE LYASE AT 2.1 ANGSTROM RESOLUTION.'''
+===CRYSTAL STRUCTURE OF STREPTOCOCCUS AGALACTIAE HYALURONATE LYASE AT 2.1 ANGSTROM RESOLUTION.===
-==Overview==
+<!--
-Streptococcus agalactiae hyaluronate lyase is a virulence factor that helps this pathogen to break through the biophysical barrier of the host tissues by the enzymatic degradation of hyaluronan and certain chondroitin sulfates at beta-1,4 glycosidic linkages. Crystal structures of the native enzyme and the enzyme-product complex were determined at 2.1- and 2.2-A resolutions, respectively. An elongated cleft transversing the middle of the molecule has been identified as the substrate-binding place. Two product molecules of hyaluronan degradation were observed bound to the cleft. The enzyme catalytic site was identified to comprise three residues: His(479), Tyr(488), and Asn(429). The highly positively charged cleft facilitates the binding of the negatively charged polymeric substrate chain. The matching between the aromatic patch of the enzyme and the hydrophobic patch of the substrate chain anchors the substrate chain into degradation position. A pair of proton exchanges between the enzyme and the substrate results in the cleavage of the beta-1,4 glycosidic linkage of the substrate chain and the unsaturation of the product. Phe(423) likely determines the size of the product at the product release side of the catalytic region. Hyaluronan chain is processively degraded from the reducing end toward the nonreducing end. The unsulfated or 6-sulfated regions of chondroitin sulfate can also be degraded in the same manner as hyaluronan.
+The line below this paragraph, {{ABSTRACT_PUBMED_11527972}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11527972 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_11527972}}
 ==About this Structure==
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 [[Category: Li, S.]]
 [[Category: The structure consists of three distinct structural domains: two beta domains at two terminals and one alpha domain in the middle of the sequence.]]
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