7x78: Difference between revisions

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-'''Unreleased structure'''
-The entry 7x78 is ON HOLD  until Paper Publication
+==L-fuculose 1-phosphate aldolase==
+<StructureSection load='7x78' size='340' side='right'caption='[[7x78]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7x78]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7X78 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7X78 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=7x78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7x78 OCA], [https://pdbe.org/7x78 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7x78 RCSB], [https://www.ebi.ac.uk/pdbsum/7x78 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7x78 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/A6TD81_KLEP7 A6TD81_KLEP7] Involved in the degradation of L-fucose and D-arabinose. Catalyzes the reversible cleavage of L-fuculose 1-phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and L-lactaldehyde.[HAMAP-Rule:MF_00987]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Fuculose phosphate aldolases play an important role in glycolysis and gluconeogenesis pathways. L-fuculose 1-phosphate aldolase catalyzes the reversible cleavage of L-fuculose 1-phosphate to DHAP and L-lactaldehyde. Class II aldolases found in bacteria are linked to pathogenesis of human pathogens, and have potential applications in the biosynthesis of carbohydrates and other chiral compounds. Here we report the structure of a putative L-fuculose 1-phosphate aldolase (KpFucA) from the nosocomial pathogen Klebsiella pneumoniae to 1.85 A resolution. The enzyme crystallizes in space group P422 with one monomer per asymmetric unit. Analytical ultracentrifugation analysis confirms that KpFucA is a tetramer in solution. A magnesium ion cofactor and sulfate ion were identified in the active pocket. Enzyme activity assays confirmed that KpFcuA has a strong preference for L-fuculose 1-phosphate as a substrate, but can also catalyze the cleavage of fructose-1,6-bisphosphate and glucose-6-phosphate. This work should provide a starting point for further investigation of the role of KpFucA in K. pneumoniae pathogenesis or in industrial applications.
-Authors: Lou, X., Zhang, Q., Bartlam, M.
+Structural characterization of an L-fuculose-1-phosphate aldolase from Klebsiella pneumoniae.,Lou X, Zhang J, Liu S, Wang R, Li W, Liu R, Zhang Q, Bartlam M Biochem Biophys Res Commun. 2022 Mar 25;607:15-19. doi:, 10.1016/j.bbrc.2022.03.127. PMID:35366538<ref>PMID:35366538</ref>
-Description: L-fuculose 1-phosphate aldolase
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Lou, X]]
+<div class="pdbe-citations 7x78" style="background-color:#fffaf0;"></div>
-[[Category: Bartlam, M]]
+== References ==
-[[Category: Zhang, Q]]
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Klebsiella pneumoniae]]
+[[Category: Large Structures]]
+[[Category: Bartlam M]]
+[[Category: Lou X]]
+[[Category: Zhang Q]]