3l8e

<StructureSection load='3l8e' size='340' side='right' caption='[[3l8e]], [[Resolution|resolution]] 1.64&Aring;' scene=''>

<table><tr><td colspan='2'>[[3l8e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L8E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3L8E FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3l8f|3l8f]], [[3l8g|3l8g]], [[3l8h|3l8h]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b0200, gmhB, JW0196, yaeD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=3l8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l8e OCA], [http://pdbe.org/3l8e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3l8e RCSB], [http://www.ebi.ac.uk/pdbsum/3l8e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3l8e ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/GMHB_ECOLI GMHB_ECOLI]] Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-beta-D-manno-heptose 1-phosphate (HBP) by removing the phosphate group at the C-7 position. Also catalyzes the dephosphorylation of fructose-1,6-bisphosphate (Fru1,6bisP).<ref>PMID:11751812</ref> <ref>PMID:16990279</ref>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l8/3l8e_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

The haloalkanoic acid dehalogenase (HAD) enzyme superfamily is the largest family of phosphohydrolases. In HAD members, the structural elements that provide the binding interactions that support substrate specificity are separated from those that orchestrate catalysis. For most HAD phosphatases, a cap domain functions in substrate recognition. However, for the HAD phosphatases that lack a cap domain, an alternate strategy for substrate selection must be operative. One such HAD phosphatase, GmhB of the HisB subfamily, was selected for structure-function analysis. Herein, the X-ray crystallographic structures of Escherichia coli GmhB in the apo form (1.6 A resolution), in a complex with Mg(2+) and orthophosphate (1.8 A resolution), and in a complex with Mg(2+) and d-glycero-d-manno-heptose 1beta,7-bisphosphate (2.2 A resolution) were determined, in addition to the structure of Bordetella bronchiseptica GmhB bound to Mg(2+) and orthophosphate (1.7 A resolution). The structures show that in place of a cap domain, the GmhB catalytic site is elaborated by three peptide inserts or loops that pack to form a concave, semicircular surface around the substrate leaving group. Structure-guided kinetic analysis of site-directed mutants was conducted in parallel with a bioinformatics study of sequence diversification within the HisB subfamily to identify loop residues that serve as substrate recognition elements and that distinguish GmhB from its subfamily counterpart, the histidinol-phosphate phosphatase domain of HisB. We show that GmhB and the histidinol-phosphate phosphatase domain use the same design of three substrate recognition loops inserted into the cap domain yet, through selective residue usage on the loops, have achieved unique substrate specificity and thus novel biochemical function.

Structural Determinants of Substrate Recognition in the HAD Superfamily Member d-glycero-d-manno-Heptose-1,7-bisphosphate Phosphatase (GmhB) .,Nguyen HH, Wang L, Huang H, Peisach E, Dunaway-Mariano D, Allen KN Biochemistry. 2010 Jan 22. PMID:20050614<ref>PMID:20050614</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3l8e" style="background-color:#fffaf0;"></div>

[[Category: Ecoli]]

[[Category: Allen, K N]]

[[Category: 7-bisphosphate phosphatase]]

[[Category: Carbohydrate metabolism]]

[[Category: Cytoplasm]]

[[Category: D-glycero-d-manno-heptose-1]]

[[Category: Gmhb]]

[[Category: Lipopolysaccharide biosynthesis]]