5wpi
From Proteopedia
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<StructureSection load='5wpi' size='340' side='right' caption='[[5wpi]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='5wpi' size='340' side='right' caption='[[5wpi]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5wpi]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WPI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WPI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5wpi]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_amylovorus"_(burrill_1882)_trevisan_1889 "bacillus amylovorus" (burrill 1882) trevisan 1889]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WPI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WPI FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hsvA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=552 "Bacillus amylovorus" (Burrill 1882) Trevisan 1889])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5wpi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wpi OCA], [http://pdbe.org/5wpi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wpi RCSB], [http://www.ebi.ac.uk/pdbsum/5wpi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wpi ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5wpi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wpi OCA], [http://pdbe.org/5wpi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wpi RCSB], [http://www.ebi.ac.uk/pdbsum/5wpi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wpi ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Studies of virulence determinants in the bacterial phytopathogen Erwinia amylovora, the cause of devastating fire blight disease in apple and pear, have shown that HsvA, a putative amidinotransferase enzyme located in the Hrp pathogenicity island, is required for systemic infection in apple. However, the mechanism by which HsvA contributes to virulence is unclear. To investigate the role of HsvA in virulence, we carried out a series of biochemical and structural studies to characterize the amidinotransferase activity of HsvA. We found that HsvA displays a preference for linear aliphatic polyamines as the amidino acceptor substrate, especially for spermidine and putrescine (KM values of 33 muM and 3.9 mM, respectively). The three-dimensional structure, determined at 2.30 A resolution using Xray crystallography, revealed that the overall architecture of HsvA is similar to that of the human arginine-glycine amidinotransferase in the creatine biosynthesis pathway. The active site is located in the core of the protein at the base of a long, narrow substrate access channel. Specific amino acids near the entrance of the channel may serve as major determinants of the substrate specificity, including a glutamate residue at the rim of the channel entrance that appears to be positioned to interact with the distal primary amine in the putrescine substrate, as well as the internal and distal amines in the spermidine substrate. These results suggest potential in vivo functions for HsvA as a virulence factor in fire blight and may also provide a basis for strategies to control fire blight by inhibiting HsvA activity. | ||
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| + | The virulence-associated protein HsvA from the fire blight pathogen Erwinia amylovora is a polyamine amidinotransferase.,Shanker S, Schaefer GK, Barnhart BK, Wallace-Kneale VL, Chang D, Coyle TJ, Metzler DA, Huang J, Lawton JA J Biol Chem. 2017 Nov 9. pii: jbc.M117.815951. doi: 10.1074/jbc.M117.815951. PMID:29123034<ref>PMID:29123034</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5wpi" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 10:32, 22 November 2017
The virulence-associated protein HsvA from the fire blight pathogen Erwinia amylovora is a polyamine amidinotransferase
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