4xxf
From Proteopedia
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<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=4xxf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xxf OCA], [http://pdbe.org/4xxf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xxf RCSB], [http://www.ebi.ac.uk/pdbsum/4xxf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xxf ProSAT]</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=4xxf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xxf OCA], [http://pdbe.org/4xxf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xxf RCSB], [http://www.ebi.ac.uk/pdbsum/4xxf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xxf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Fuculose-1-phosphate aldolase (FucA) catalyses the reversible cleavage of L-fuculose 1-phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde. This enzyme from mesophiles and thermophiles has been extensively studied; however, there is no report on this enzyme from a psychrophile. In this study, the gene encoding FucA from Glaciozyma antarctica PI12 (GaFucA) was cloned and the enzyme was overexpressed in Escherichia coli, purified and crystallized. The tetrameric structure of GaFucA was determined to 1.34 A resolution. The overall architecture of GaFucA and its catalytically essential histidine triad are highly conserved among other fuculose aldolases. Comparisons of structural features between GaFucA and its mesophilic and thermophilic homologues revealed that the enzyme has typical psychrophilic attributes, indicated by the presence of a high number of nonpolar residues at the surface and a lower number of arginine residues. | ||
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| + | Crystal structure of fuculose aldolase from the Antarctic psychrophilic yeast Glaciozyma antarctica PI12.,Jaafar NR, Littler D, Beddoe T, Rossjohn J, Illias RM, Mahadi NM, Mackeen MM, Murad AM, Abu Bakar FD Acta Crystallogr F Struct Biol Commun. 2016 Nov 1;72(Pt 11):831-839. doi:, 10.1107/S2053230X16015612. Epub 2016 Oct 27. PMID:27827354<ref>PMID:27827354</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4xxf" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Aldolase 3D structures|Aldolase 3D structures]] | *[[Aldolase 3D structures|Aldolase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 10:41, 25 December 2019
L-fuculose 1-phosphate aldolase from Glaciozyma antarctica PI12
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