1c82
From Proteopedia
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|PDB= 1c82 |SIZE=350|CAPTION= <scene name='initialview01'>1c82</scene>, resolution 1.7Å | |PDB= 1c82 |SIZE=350|CAPTION= <scene name='initialview01'>1c82</scene>, resolution 1.7Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene> | + | |LIGAND= <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=DGC:D-GLUCURONIC+ACID'>DGC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Hyaluronate_lyase Hyaluronate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.1 4.2.2.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Hyaluronate_lyase Hyaluronate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.1 4.2.2.1] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c82 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c82 OCA], [http://www.ebi.ac.uk/pdbsum/1c82 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1c82 RCSB]</span> | ||
}} | }} | ||
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[[Category: Jedrzejas, M J.]] | [[Category: Jedrzejas, M J.]] | ||
[[Category: Ponnuraj, K.]] | [[Category: Ponnuraj, K.]] | ||
| - | [[Category: CAC]] | ||
| - | [[Category: NA]] | ||
[[Category: protein-carbohydrate complex]] | [[Category: protein-carbohydrate complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:16:29 2008'' |
Revision as of 16:16, 30 March 2008
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| , resolution 1.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Activity: | Hyaluronate lyase, with EC number 4.2.2.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
MECHANISM OF HYALURONAN BINDING AND DEGRADATION: STRUCTURE OF STREPTOCOCCUS PNEUMONIAE HYALURONATE LYASE IN COMPLEX WITH HYALURONIC ACID DISACCHARIDE AT 1.7 A RESOLUTION
Overview
Hyaluronic acid (HA) is an important constituent of the extracellular matrix; its bacterial degradation has been postulated to contribute to the spread of certain streptococci through tissue. Pneumococci and other streptococci produce hyaluronate lyase, an enzyme which depolymerizes HA, thus hyaluronate lyase might contribute directly to bacterial invasion. Although two different mechanisms for lyase action have been proposed, there was no crystallographic evidence to support those mechanisms. Here, we report the high-resolution crystal structure of Streptococcus pneumoniae hyaluronate lyase in the presence of HA disaccharide product, which ultimately provides the first crystallographic evidence for the binding of HA to hyaluronate lyase. This structural complex revealed a key interaction between the Streptococcus peneumoniae hyaluronate lyase protein and the product, and supports our previously proposed novel catalytic mechanism for HA degradation based on the native Streptococcus peneumoniae hyaluronate lyase structure. The information provided by this complex structure will likely be useful in the development of antimicrobial pharmaceutical agents.
About this Structure
1C82 is a Single protein structure of sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA.
Reference
Mechanism of hyaluronan binding and degradation: structure of Streptococcus pneumoniae hyaluronate lyase in complex with hyaluronic acid disaccharide at 1.7 A resolution., Ponnuraj K, Jedrzejas MJ, J Mol Biol. 2000 Jun 16;299(4):885-95. PMID:10843845
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