2ajt: Difference between revisions
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==Crystal structure of L-Arabinose Isomerase from E.coli== | ==Crystal structure of L-Arabinose Isomerase from E.coli== | ||
<StructureSection load='2ajt' size='340' side='right' caption='[[2ajt]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='2ajt' size='340' side='right' caption='[[2ajt]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">araA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">araA ([http://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'>[http://en.wikipedia.org/wiki/L-arabinose_isomerase L-arabinose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.4 5.3.1.4] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-arabinose_isomerase L-arabinose isomerase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ajt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ajt OCA], [http://pdbe.org/2ajt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ajt RCSB], [http://www.ebi.ac.uk/pdbsum/2ajt PDBsum], [http://www.topsan.org/Proteins/NYSGXRC/2ajt TOPSAN]</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=2ajt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ajt OCA], [http://pdbe.org/2ajt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ajt RCSB], [http://www.ebi.ac.uk/pdbsum/2ajt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ajt ProSAT], [http://www.topsan.org/Proteins/NYSGXRC/2ajt TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aj/2ajt_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aj/2ajt_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 10:02, 9 May 2018
Crystal structure of L-Arabinose Isomerase from E.coliCrystal structure of L-Arabinose Isomerase from E.coli
Structural highlights
Function[ARAA_ECOLI] Catalyzes the conversion of L-arabinose to L-ribulose.[HAMAP-Rule:MF_00519] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedEscherichia 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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