2ajt: Difference between revisions

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 <StructureSection load='2ajt' size='340' side='right'caption='[[2ajt]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ajt]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AJT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AJT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ajt]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AJT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AJT FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fui|1fui]]</div></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">araA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/L-arabinose_isomerase L-arabinose isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.4 5.3.1.4] </span></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=2ajt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ajt OCA], [https://pdbe.org/2ajt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ajt RCSB], [https://www.ebi.ac.uk/pdbsum/2ajt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ajt ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/2ajt TOPSAN]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/ARAA_ECOLI ARAA_ECOLI]] Catalyzes the conversion of L-arabinose to L-ribulose.[HAMAP-Rule:MF_00519]
+[https://www.uniprot.org/uniprot/ARAA_ECOLI ARAA_ECOLI] Catalyzes the conversion of L-arabinose to L-ribulose.[HAMAP-Rule:MF_00519]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </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/main_output.php?pdb_ID=2ajt ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Escherichia coli L-arabinose isomerase (ECAI; EC 5.3.1.4) catalyzes the isomerization of L-arabinose to L-ribulose in vivo. This enzyme is also of commercial interest as it catalyzes the conversion of D-galactose to D-tagatose in vitro. The crystal structure of ECAI was solved and refined at 2.6 A resolution. The subunit structure of ECAI is organised into three domains: an N-terminal, a central and a C-terminal domain. It forms a crystallographic trimeric architecture in the asymmetric unit. Packing within the crystal suggests the idea that ECAI can form a hexameric assembly. Previous electron microscopic and biochemical studies supports that ECAI is hexameric in solution. A comparison with other known structures reveals that ECAI adopts a protein fold most similar to E. coli fucose isomerase (ECFI) despite very low sequence identity 9.7%. The structural similarity between ECAI and ECFI with regard to number of domains, overall fold, biological assembly, and active site architecture strongly suggests that the enzymes have functional similarities. Further, the crystal structure of ECAI forms a basis for identifying molecular determinants responsible for isomerization of arabinose to ribulose in vivo and galactose to tagatose in vitro.
-Crystal structure of Escherichia coli L-arabinose isomerase (ECAI), the putative target of biological tagatose production.,Manjasetty BA, Chance MR J Mol Biol. 2006 Jul 7;360(2):297-309. Epub 2006 May 5. PMID:16756997<ref>PMID:16756997</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2ajt" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
-[[Category: L-arabinose isomerase]]
 [[Category: Large Structures]]
-[[Category: Almo, S C]]
+[[Category: Almo SC]]
-[[Category: Burley, S K]]
+[[Category: Burley SK]]
-[[Category: Chance, M R]]
+[[Category: Chance MR]]
-[[Category: Fedorov, E V]]
+[[Category: Fedorov EV]]
-[[Category: Manjasetty, B A]]
+[[Category: Manjasetty BA]]
-[[Category: Structural genomic]]
-[[Category: Arabinose catabolism]]
-[[Category: Carbohydrate metabolism]]
-[[Category: Isomerase]]
-[[Category: NYSGXRC, New York SGX Research Center for Structural Genomics]]
-[[Category: PSI, Protein structure initiative]]