1egu: Difference between revisions
New page: left|200px<br /><applet load="1egu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1egu, resolution 1.56Å" /> '''CRYSTAL STRUCTURE OF... |
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[[Image:1egu.gif|left|200px]]<br /><applet load="1egu" size=" | [[Image:1egu.gif|left|200px]]<br /><applet load="1egu" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1egu, resolution 1.56Å" /> | caption="1egu, resolution 1.56Å" /> | ||
'''CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE HYALURONATE LYASE AT 1.56 A RESOLUTION'''<br /> | '''CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE HYALURONATE LYASE AT 1.56 A RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
Streptococcus pneumoniae hyaluronate lyase (spnHL) is a pathogenic | Streptococcus pneumoniae hyaluronate lyase (spnHL) is a pathogenic bacterial spreading factor and cleaves hyaluronan, an important constituent of the extra- cellular matrix of connective tissues, through an enzymatic beta-elimination process, different from the hyaluronan degradation by hydrolases in animals. The mechanism of hyaluronan binding and degradation was proposed based on the 1.56 A resolution crystal structure, substrate modeling and mutagenesis studies on spnHL. Five mutants, R243V, N349A, H399A, Y408F and N580G, were constructed and their activities confirmed our mechanism hypothesis. The important roles of Tyr408, Asn349 and His399 in enzyme catalysis were proposed, explained and confirmed by mutant studies. The remaining weak enzymatic activity of the H399A mutant, the role of the free carboxylate group on the glucuronate residue, the enzymatic behavior on chondroitin and chondroitin sulfate, and the small activity increase in the N580G mutant were explained based on this mechanism. A possible function of the C-terminal beta-sheet domain is to modulate enzyme activity through binding to calcium ions. | ||
==About this Structure== | ==About this Structure== | ||
1EGU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | 1EGU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EGU OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Streptococcus pneumoniae]] | [[Category: Streptococcus pneumoniae]] | ||
[[Category: Ferraroni, M.]] | [[Category: Ferraroni, M.]] | ||
[[Category: Jedrzejas, M | [[Category: Jedrzejas, M J.]] | ||
[[Category: Kelly, S | [[Category: Kelly, S J.]] | ||
[[Category: Lamani, E.]] | [[Category: Lamani, E.]] | ||
[[Category: Li, S.]] | [[Category: Li, S.]] | ||
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[[Category: (alfa5/alfa5) barrel]] | [[Category: (alfa5/alfa5) barrel]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:27:36 2008'' | ||
Revision as of 13:27, 21 February 2008
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CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE HYALURONATE LYASE AT 1.56 A RESOLUTION
OverviewOverview
Streptococcus pneumoniae hyaluronate lyase (spnHL) is a pathogenic bacterial spreading factor and cleaves hyaluronan, an important constituent of the extra- cellular matrix of connective tissues, through an enzymatic beta-elimination process, different from the hyaluronan degradation by hydrolases in animals. The mechanism of hyaluronan binding and degradation was proposed based on the 1.56 A resolution crystal structure, substrate modeling and mutagenesis studies on spnHL. Five mutants, R243V, N349A, H399A, Y408F and N580G, were constructed and their activities confirmed our mechanism hypothesis. The important roles of Tyr408, Asn349 and His399 in enzyme catalysis were proposed, explained and confirmed by mutant studies. The remaining weak enzymatic activity of the H399A mutant, the role of the free carboxylate group on the glucuronate residue, the enzymatic behavior on chondroitin and chondroitin sulfate, and the small activity increase in the N580G mutant were explained based on this mechanism. A possible function of the C-terminal beta-sheet domain is to modulate enzyme activity through binding to calcium ions.
About this StructureAbout this Structure
1EGU is a Single protein structure of sequence from Streptococcus pneumoniae with as ligand. Active as Hyaluronate lyase, with EC number 4.2.2.1 Full crystallographic information is available from OCA.
ReferenceReference
Structural basis of hyaluronan degradation by Streptococcus pneumoniae hyaluronate lyase., Li S, Kelly SJ, Lamani E, Ferraroni M, Jedrzejas MJ, EMBO J. 2000 Mar 15;19(6):1228-40. PMID:10716923
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