3o82: Difference between revisions
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==Structure of BasE N-terminal domain from Acinetobacter baumannii bound to 5'-O-[N-(2,3-dihydroxybenzoyl)sulfamoyl] adenosine== | |||
<StructureSection load='3o82' size='340' side='right' caption='[[3o82]], [[Resolution|resolution]] 2.70Å' scene=''> | |||
{ | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3o82]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Acinetobacter_baumannii Acinetobacter baumannii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O82 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O82 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HP8:5-O-{[(2,3-DIHYDROXYPHENYL)CARBONYL]SULFAMOYL}ADENOSINE'>HP8</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3o83|3o83]], [[3o84|3o84]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACICU_02578, basE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=470 Acinetobacter baumannii])</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=3o82 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o82 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o82 RCSB], [http://www.ebi.ac.uk/pdbsum/3o82 PDBsum]</span></td></tr> | |||
</table> | |||
== 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/o8/3o82_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/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The human pathogen Acinetobacter baumannii produces a siderophore called acinetobactin that is derived from one molecule each of threonine, histidine, and 2,3-dihydroxybenzoic acid (DHB). The activity of several non-ribosomal peptide synthetase (NRPS) enzymes is used to combine the building blocks into the final molecule. The acinetobactin synthesis pathway initiates with a self-standing adenylation enzyme, BasE, that activates the DHB molecule and covalently transfers it to the pantetheine cofactor of an aryl-carrier protein of BasF, a strategy that is shared with many siderophore-producing NRPS clusters. In this reaction, DHB reacts with ATP to form the aryl adenylate and pyrophosphate. In a second partial reaction, the DHB is transferred to the carrier protein. Inhibitors of BasE and related enzymes have been identified that prevent growth of bacteria on iron-limiting media. Recently, a new inhibitor of BasE has been identified via high-throughput screening using a fluorescence polarization displacement assay. We present here biochemical and structural studies to examine the binding mode of this inhibitor. The kinetics of the wild-type BasE enzyme is shown and inhibition studies demonstrate that the new compound exhibits competitive inhibition against both ATP and 2,3-dihydroxybenzoate. Structural examination of BasE bound to this inhibitor illustrates a novel binding mode in which the phenyl moiety partially fills the enzyme pantetheine binding tunnel. Structures of rationally designed bisubstrate inhibitors are also presented. | |||
Biochemical and Structural Characterization of Bisubstrate Inhibitors of BasE, the Self-standing Non-Ribosomal Peptide Synthetase Adenylate-Forming Enzyme of Acinetobactin Synthesis.,Drake EJ, Duckworth BP, Neres J, Aldrich CC, Gulick AM Biochemistry. 2010 Sep 20. PMID:20853905<ref>PMID:20853905</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Acinetobacter baumannii]] | [[Category: Acinetobacter baumannii]] | ||
[[Category: Aldrich, C C | [[Category: Aldrich, C C]] | ||
[[Category: Drake, E J | [[Category: Drake, E J]] | ||
[[Category: Duckworth, B P | [[Category: Duckworth, B P]] | ||
[[Category: Gulick, A M | [[Category: Gulick, A M]] | ||
[[Category: Neres, J | [[Category: Neres, J]] | ||
[[Category: 3-dihydroxybenzoate and transfer to pantetheine cofactor of basf]] | [[Category: 3-dihydroxybenzoate and transfer to pantetheine cofactor of basf]] | ||
[[Category: Adenylation of 2]] | [[Category: Adenylation of 2]] | ||
[[Category: Ligase]] | [[Category: Ligase]] | ||
