2x3h: Difference between revisions
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< | ==COLIPHAGE K5A LYASE== | ||
<StructureSection load='2x3h' size='340' side='right'caption='[[2x3h]], [[Resolution|resolution]] 1.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2x3h]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_K1-5 Escherichia virus K1-5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X3H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X3H FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> | |||
-- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2x3h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x3h OCA], [https://pdbe.org/2x3h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x3h RCSB], [https://www.ebi.ac.uk/pdbsum/2x3h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x3h ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/O09496_9CAUD O09496_9CAUD] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
K5 lyase A (KflA) is a tail spike protein (TSP) encoded by a K5A coliphage, which cleaves K5 capsular polysaccharide, a glycosaminoglycan with the repeat unit [-4)-betaGlcA-(1,4)- alphaGlcNAc(1-], displayed on the surface of Escherichia coli K5 strains. The crystal structure of KflA reveals a trimeric arrangement, with each monomer containing a right-handed, single-stranded parallel beta-helix domain. Stable trimer formation by the intertwining of strands in the C-terminal domain, followed by proteolytic maturation, is likely to be catalyzed by an autochaperone as described for K1F endosialidase. The structure of KflA represents the first bacteriophage tail spike protein combining polysaccharide lyase activity with a single-stranded parallel beta-helix fold. We propose a catalytic site and mechanism representing convergence with the syn-beta-elimination site of heparinase II from Pedobacter heparinus. | |||
The K5 lyase KflA combines a viral tail spike structure with a bacterial polysaccharide lyase mechanism.,Thompson JE, Pourhossein M, Waterhouse A, Hudson T, Goldrick M, Derrick JP, Roberts IS J Biol Chem. 2010 Jul 30;285(31):23963-9. Epub 2010 Jun 2. PMID:20519506<ref>PMID:20519506</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
== | </div> | ||
<div class="pdbe-citations 2x3h" style="background-color:#fffaf0;"></div> | |||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: Derrick | __TOC__ | ||
[[Category: Goldrick | </StructureSection> | ||
[[Category: Hudson | [[Category: Escherichia virus K1-5]] | ||
[[Category: Pourhossein | [[Category: Large Structures]] | ||
[[Category: Roberts | [[Category: Derrick JP]] | ||
[[Category: Thompson | [[Category: Goldrick M]] | ||
[[Category: Hudson T]] | |||
[[Category: Pourhossein M]] | |||
[[Category: Roberts IS]] | |||
[[Category: Thompson JE]] | |||
Latest revision as of 10:17, 9 August 2023
COLIPHAGE K5A LYASECOLIPHAGE K5A LYASE
Structural highlights
FunctionPublication Abstract from PubMedK5 lyase A (KflA) is a tail spike protein (TSP) encoded by a K5A coliphage, which cleaves K5 capsular polysaccharide, a glycosaminoglycan with the repeat unit [-4)-betaGlcA-(1,4)- alphaGlcNAc(1-], displayed on the surface of Escherichia coli K5 strains. The crystal structure of KflA reveals a trimeric arrangement, with each monomer containing a right-handed, single-stranded parallel beta-helix domain. Stable trimer formation by the intertwining of strands in the C-terminal domain, followed by proteolytic maturation, is likely to be catalyzed by an autochaperone as described for K1F endosialidase. The structure of KflA represents the first bacteriophage tail spike protein combining polysaccharide lyase activity with a single-stranded parallel beta-helix fold. We propose a catalytic site and mechanism representing convergence with the syn-beta-elimination site of heparinase II from Pedobacter heparinus. The K5 lyase KflA combines a viral tail spike structure with a bacterial polysaccharide lyase mechanism.,Thompson JE, Pourhossein M, Waterhouse A, Hudson T, Goldrick M, Derrick JP, Roberts IS J Biol Chem. 2010 Jul 30;285(31):23963-9. Epub 2010 Jun 2. PMID:20519506[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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