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| | ==Crystal Structure of Calcium-bound D,D-heptose 1.7-bisphosphate phosphatase from E. Coli== | | ==Crystal Structure of Calcium-bound D,D-heptose 1.7-bisphosphate phosphatase from E. Coli== |
| - | <StructureSection load='3esq' size='340' side='right' caption='[[3esq]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='3esq' size='340' side='right'caption='[[3esq]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3esq]] is a 1 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=3ESQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ESQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3esq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ESQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ESQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3esr|3esr]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=3esq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3esq OCA], [https://pdbe.org/3esq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3esq RCSB], [https://www.ebi.ac.uk/pdbsum/3esq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3esq 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=3esq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3esq OCA], [http://pdbe.org/3esq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3esq RCSB], [http://www.ebi.ac.uk/pdbsum/3esq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3esq ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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> | + | [https://www.uniprot.org/uniprot/GMHBB_ECOLI GMHBB_ECOLI] Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate (beta-HBP) intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.<ref>PMID:11751812</ref> <ref>PMID:16990279</ref> <ref>PMID:20050615</ref> <ref>PMID:31449400</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Junop, M S]]
| + | [[Category: Large Structures]] |
| - | [[Category: Sugiman-Marangos, S N]]
| + | [[Category: Junop MS]] |
| - | [[Category: Carbohydrate metabolism]] | + | [[Category: Sugiman-Marangos SN]] |
| - | [[Category: Hydrolase]] | + | |
| - | [[Category: Lipopolysaccharide biosynthesis]] | + | |
| Structural highlights
Function
GMHBB_ECOLI Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate (beta-HBP) intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.[1] [2] [3] [4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Kneidinger B, Marolda C, Graninger M, Zamyatina A, McArthur F, Kosma P, Valvano MA, Messner P. Biosynthesis pathway of ADP-L-glycero-beta-D-manno-heptose in Escherichia coli. J Bacteriol. 2002 Jan;184(2):363-9. PMID:11751812
- ↑ Kuznetsova E, Proudfoot M, Gonzalez CF, Brown G, Omelchenko MV, Borozan I, Carmel L, Wolf YI, Mori H, Savchenko AV, Arrowsmith CH, Koonin EV, Edwards AM, Yakunin AF. Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family. J Biol Chem. 2006 Nov 24;281(47):36149-61. Epub 2006 Sep 21. PMID:16990279 doi:10.1074/jbc.M605449200
- ↑ Wang L, Huang H, Nguyen HH, Allen KN, Mariano PS, Dunaway-Mariano D. Divergence of biochemical function in the HAD superfamily: D-glycero-D-manno-heptose-1,7-bisphosphate phosphatase (GmhB). Biochemistry. 2010 Feb 16;49(6):1072-81. doi: 10.1021/bi902018y. PMID:20050615 doi:http://dx.doi.org/10.1021/bi902018y
- ↑ Huddleston JP, Raushel FM. Biosynthesis of GDP-d-glycero-alpha-d-manno-heptose for the Capsular Polysaccharide of Campylobacter jejuni. Biochemistry. 2019 Sep 17;58(37):3893-3902. doi: 10.1021/acs.biochem.9b00548. , Epub 2019 Aug 29. PMID:31449400 doi:http://dx.doi.org/10.1021/acs.biochem.9b00548
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