2kwl

<StructureSection load='2kwl' size='340' side='right' caption='[[2kwl]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[2kwl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Borrelia_burgdorferi Borrelia burgdorferi]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KWL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KWL FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">acpP, BB_0704 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=139 Borrelia burgdorferi])</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=2kwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kwl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2kwl RCSB], [http://www.ebi.ac.uk/pdbsum/2kwl PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/ACP_BORBU ACP_BORBU]] Carrier of the growing fatty acid chain in fatty acid biosynthesis (By similarity).

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kw/2kwl_consurf.spt"</scriptWhenChecked>

</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="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Nearly complete resonance assignment and the high-resolution NMR structure of the acyl-carrier protein from Borrelia burgdorferi, a target of the Seattle Structural Genomics Center for Infectious Disease (SSGCID) structure-determination pipeline, are reported. This protein was chosen as a potential target for drug-discovery efforts because of its involvement in fatty-acid biosynthesis, an essential metabolic pathway, in bacteria. It was possible to assign &gt;98% of backbone resonances and &gt;92% of side-chain resonances using multidimensional NMR spectroscopy. The NMR structure was determined to a backbone r.m.s.d. of 0.4 A and contained four alpha-helices and two 3(10)-helices. A structure-homology search revealed that this protein is highly similar to the acyl-carrier protein from Aquifex aeolicus.

NMR structure of an acyl-carrier protein from Borrelia burgdorferi.,Barnwal RP, Van Voorhis WC, Varani G Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt, 9):1137-40. Epub 2011 Aug 13. PMID:21904063<ref>PMID:21904063</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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*[[Acyl carrier protein|Acyl carrier protein]]

[[Category: Borrelia burgdorferi]]

[[Category: Barnwal, R]]

[[Category: Moody, J]]

[[Category: Structural genomic]]

[[Category: Varani, G]]

[[Category: Vittal, V]]

[[Category: Ssgcid]]