1sjw

<StructureSection load='1sjw' size='340' side='right' caption='[[1sjw]], [[Resolution|resolution]] 1.35&Aring;' scene=''>

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

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NGV:METHYL+5,7-DIHYDROXY-2-METHYL-4,6,11-TRIOXO-3,4,6,11-TETRAHYDROTETRACENE-1-CARBOXYLATE'>NGV</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SnoaL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=38314 Streptomyces nogalater])</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=1sjw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sjw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1sjw RCSB], [http://www.ebi.ac.uk/pdbsum/1sjw PDBsum]</span></td></tr>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sj/1sjw_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].

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== Publication Abstract from PubMed ==

SnoaL belongs to a family of small polyketide cyclases, which catalyse ring closure steps in the biosynthesis of polyketide antibiotics produced in Streptomyces. Several of these antibiotics are among the most used anti-cancer drugs currently in use. The crystal structure of SnoaL, involved in nogalamycin biosynthesis, with a bound product, has been determined to 1.35 A resolution. The fold of the subunit can be described as a distorted alpha+beta barrel, and the ligand is bound in the hydrophobic interior of the barrel. The 3D structure and site-directed mutagenesis experiments reveal that the mechanism of the intramolecular aldol condensation catalysed by SnoaL is different from that of the classical aldolases, which employ covalent Schiff base formation or a metal ion cofactor. The invariant residue Asp121 acts as an acid/base catalyst during the reaction. Stabilisation of the enol(ate) intermediate is mainly achieved by the delocalisation of the electron pair over the extended pi system of the substrate. These polyketide cyclases thus form of family of enzymes with a unique catalytic strategy for aldol condensation.

Structure of the polyketide cyclase SnoaL reveals a novel mechanism for enzymatic aldol condensation.,Sultana A, Kallio P, Jansson A, Wang JS, Niemi J, Mantsala P, Schneider G EMBO J. 2004 May 5;23(9):1911-21. Epub 2004 Apr 8. PMID:15071504<ref>PMID:15071504</ref>

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

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[[Category: Jansson, A]]

[[Category: Kallio, P]]

[[Category: Mantsala, P]]

[[Category: Neimi, J]]

[[Category: SPINE, Structural Proteomics in Europe]]

[[Category: Schneider, G]]

[[Category: Sultana, A]]

[[Category: Wang, J S]]

[[Category: Structural proteomics in europe]]