2brw: Difference between revisions

Revision as of 05:34, 28 July 2008

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File:2brw.png

Template:STRUCTURE 2brw

CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE HYALURONATE LYASE FROM 30PERCENT PEGMME.CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE HYALURONATE LYASE FROM 30PERCENT PEGMME.

Template:ABSTRACT PUBMED 16569416

About this StructureAbout this Structure

2BRW is a Single protein structure of sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA.

ReferenceReference

Alternate structural conformations of Streptococcus pneumoniae hyaluronan lyase: insights into enzyme flexibility and underlying molecular mechanism of action., Rigden DJ, Littlejohn JE, Joshi HV, de Groot BL, Jedrzejas MJ, J Mol Biol. 2006 May 12;358(4):1165-78. Epub 2006 Mar 13. PMID:16569416

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE HYALURONATE LYASE FROM 30PERCENT PEGMME.'''
+===CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE HYALURONATE LYASE FROM 30PERCENT PEGMME.===
-==Overview==
+<!--
-Streptococcus pneumoniae hyaluronan lyase is a surface enzyme of this Gram-positive bacterium. The enzyme degrades several biologically important, information-rich linear polymeric glycans: hyaluronan, unsulfated chondroitin, and some chondroitin sulfates. This degradation facilitates spreading of bacteria throughout the host tissues and presumably provides energy and a carbon source for pneumococcal cells. Its beta-elimination catalytic mechanism is an acid/base process termed proton acceptance and donation leading to cleavage of beta-1,4 linkages of the substrates. The degradation of hyaluronan occurs in two stages, initial endolytic cuts are followed by processive exolytic cleavage of one disaccharide at a time. In contrast, the degradation of chondroitins is purely endolytic. Structural studies together with flexibility analyses of two streptococcal enzymes, from S.pneumoniae and Streptococcus agalactiae, allowed for insights into this enzyme's molecular mechanism. Here, two new X-ray crystal structures of the pneumococcal enzyme in novel conformations are reported. These new conformations, complemented by molecular dynamics simulation results, directly confirm the predicted domain motions presumed to facilitate the processive degradative process. One of these new structures resembles the S.agalactiae enzyme conformation, and provides evidence of a uniform mechanistic/dynamic behavior of this protein across different bacteria.
+The line below this paragraph, {{ABSTRACT_PUBMED_16569416}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16569416 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16569416}}
 ==About this Structure==
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 [[Category: Lyase]]
 [[Category: Peptidoglycan-anchor]]
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