1f9g: Difference between revisions

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[[Image:1f9g.gif|left|200px]]
{{Seed}}
[[Image:1f9g.png|left|200px]]


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{{STRUCTURE_1f9g|  PDB=1f9g  |  SCENE=  }}  
{{STRUCTURE_1f9g|  PDB=1f9g  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE HYALURONATE LYASE COCRYSTALLIZED WITH ASCORBIC ACID'''
===CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE HYALURONATE LYASE COCRYSTALLIZED WITH ASCORBIC ACID===




==Overview==
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Enzyme activity measurement showed that L-ascorbic acid (vitamin C (Vc)) competitively inhibits the hyaluronan degradation by Streptococcus pneumoniae hyaluronate lyase. The complex crystal structure of this enzyme with Vc was determined at 2.0 A resolution. One Vc molecule was found to bind to the active site of the enzyme. The Vc carboxyl group provides the negative charges that lead the molecule into the highly positively charged cleft of the enzyme. The Vc ring system forms hydrophobic interactions with the side chain of Trp-292, which is one of the aromatic patch residues of this enzyme responsible for the selection of the cleavage sites on the substrate chain. The binding of Vc inhibits the substrate binding at hyaluronan 1, 2, and 3 (HA1, HA2, and HA3) catalytic positions. The high concentration of Vc in human tissues probably provides a low level of natural resistance to the pneumococcal invasion. This is the first time that Vc the direct inhibition on the bacterial "spreading factor" was reported, and Vc is also the first chemical that has been shown experimentally to have an inhibitory effect on bacterial hyaluronate lyase. These studies also highlight the possible structural requirement for the design of a stronger inhibitor of bacterial hyaluronate lyase.
The line below this paragraph, {{ABSTRACT_PUBMED_11278838}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 11278838 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11278838}}


==About this Structure==
==About this Structure==
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[[Category: Signal]]
[[Category: Signal]]
[[Category: Transmembrane]]
[[Category: Transmembrane]]
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