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[[Image:1f1s.jpg|left|200px]]


{{Structure
==CRYSTAL STRUCTURE OF STREPTOCOCCUS AGALACTIAE HYALURONATE LYASE AT 2.1 ANGSTROM RESOLUTION.==
|PDB= 1f1s |SIZE=350|CAPTION= <scene name='initialview01'>1f1s</scene>, resolution 2.1&Aring;
<StructureSection load='1f1s' size='340' side='right'caption='[[1f1s]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1f1s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_agalactiae Streptococcus agalactiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F1S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F1S FirstGlance]. <br>
|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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f1s OCA], [https://pdbe.org/1f1s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f1s RCSB], [https://www.ebi.ac.uk/pdbsum/1f1s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f1s ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=[[1i8q|1I8Q]]
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f1s OCA], [http://www.ebi.ac.uk/pdbsum/1f1s PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1f1s RCSB]</span>
[https://www.uniprot.org/uniprot/HYSA_STRA3 HYSA_STRA3]
}}
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f1/1f1s_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1f1s ConSurf].
<div style="clear:both"></div>


'''CRYSTAL STRUCTURE OF STREPTOCOCCUS AGALACTIAE HYALURONATE LYASE AT 2.1 ANGSTROM RESOLUTION.'''
==See Also==
 
*[[Hyaluronidase 3D structures|Hyaluronidase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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.
[[Category: Large Structures]]
 
==About this Structure==
1F1S is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_agalactiae Streptococcus agalactiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F1S OCA].
 
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/11527972 11527972]
[[Category: Hyaluronate lyase]]
[[Category: Single protein]]
[[Category: Streptococcus agalactiae]]
[[Category: Streptococcus agalactiae]]
[[Category: Jedrzejas, M J.]]
[[Category: Jedrzejas MJ]]
[[Category: Li, S.]]
[[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.]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:14:10 2008''

Latest revision as of 10:09, 7 February 2024

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

Structural highlights

1f1s is a 1 chain structure with sequence from Streptococcus agalactiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HYSA_STRA3

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1f1s, resolution 2.10Å

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