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2xhz

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[[Image:2xhz.jpg|left|200px]]
 
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==Probing the active site of the sugar isomerase domain from E. coli arabinose-5-phosphate isomerase via X-ray crystallography==
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The line below this paragraph, containing "STRUCTURE_2xhz", creates the "Structure Box" on the page.
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<StructureSection load='2xhz' size='340' side='right'caption='[[2xhz]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2xhz]] is a 4 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=2XHZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XHZ FirstGlance]. <br>
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</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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xhz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xhz OCA], [https://pdbe.org/2xhz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xhz RCSB], [https://www.ebi.ac.uk/pdbsum/2xhz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xhz ProSAT]</span></td></tr>
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{{STRUCTURE_2xhz| PDB=2xhz | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/KDSD_ECOLI KDSD_ECOLI] Involved in the biosynthesis of 3-deoxy-D-manno-octulosonate (KDO), a unique 8-carbon sugar component of lipopolysaccharides (LPSs). KdsD is not essential in the KDO biosynthesis and can be substituted by GutQ. Catalyzes the reversible aldol-ketol isomerization between D-ribulose 5-phosphate (Ru5P) and D-arabinose 5-phosphate (A5P).<ref>PMID:12805358</ref> <ref>PMID:16199563</ref> <ref>PMID:16765569</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Lipopolysaccharide (LPS) biosynthesis represents an underexploited target pathway for novel antimicrobial development to combat the emergence of multidrug-resistant bacteria. A key player in LPS synthesis is the enzyme D-arabinose-5-phosphate isomerase (API), which catalyzes the reversible isomerization of D-ribulose-5-phosphate to D-arabinose-5-phosphate, a precursor of 3-deoxy-D-manno-octulosonate that is an essential residue of the LPS inner core. API is composed of two main domains: an N-terminal sugar isomerase domain (SIS) and a pair of cystathionine-beta-synthase domains of unknown function. As the three-dimensional structure of an enzyme is a prerequisite for the rational development of novel inhibitors, we present here the crystal structure of the SIS domain of a catalytic mutant (K59A) of E. coli D-arabinose-5-phosphate isomerase at 2.6-A resolution. Our structural analyses and comparisons made with other SIS domains highlight several potentially important active site residues. In particular, the crystal structure allowed us to identify a previously unpredicted His residue (H88) located at the mouth of the active site cavity as a possible catalytic residue. On the basis of such structural data, subsequently supported by biochemical and mutational experiments, we confirm the catalytic role of H88, which appears to be a generally conserved residue among two-domain isomerases.
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===PROBING THE ACTIVE SITE OF THE SUGAR ISOMERASE DOMAIN FROM E. COLI ARABINOSE-5-PHOSPHATE ISOMERASE VIA X-RAY CRYSTALLOGRAPHY===
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Probing the active site of the sugar isomerase domain from E. coli arabinose-5-phosphate isomerase via X-ray crystallography.,Gourlay LJ, Sommaruga S, Nardini M, Sperandeo P, Deho G, Polissi A, Bolognesi M Protein Sci. 2010 Dec;19(12):2430-9. doi: 10.1002/pro.525. PMID:20954237<ref>PMID:20954237</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_20954237}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2xhz" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20954237 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20954237}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[2xhz]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XHZ OCA].
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==Reference==
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<ref group="xtra">PMID:20954237</ref><references group="xtra"/>
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[[Category: Arabinose-5-phosphate isomerase]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Bolognesi, M.]]
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[[Category: Large Structures]]
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[[Category: Deho, G.]]
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[[Category: Bolognesi M]]
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[[Category: Gourlay, L J.]]
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[[Category: Deho G]]
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[[Category: Nardini, M.]]
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[[Category: Gourlay LJ]]
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[[Category: Polissi, A.]]
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[[Category: Nardini M]]
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[[Category: Sommaruga, S.]]
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[[Category: Polissi A]]
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[[Category: Sperandeo, P.]]
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[[Category: Sommaruga S]]
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[[Category: Sperandeo P]]

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Probing the active site of the sugar isomerase domain from E. coli arabinose-5-phosphate isomerase via X-ray crystallography

PDB ID 2xhz

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