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| | <StructureSection load='1sz2' size='340' side='right'caption='[[1sz2]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='1sz2' size='340' side='right'caption='[[1sz2]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1sz2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SZ2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1SZ2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1sz2]] is a 2 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=1SZ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SZ2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</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]] 2.2Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1q18|1q18]]</div></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=1sz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sz2 OCA], [https://pdbe.org/1sz2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sz2 RCSB], [https://www.ebi.ac.uk/pdbsum/1sz2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sz2 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GLK, B2388, Z3654, ECS3268 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1sz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sz2 OCA], [http://pdbe.org/1sz2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sz2 RCSB], [http://www.ebi.ac.uk/pdbsum/1sz2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1sz2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GLK_ECOLI GLK_ECOLI]] Not highly important in E.coli as glucose is transported into the cell by the PTS system already as glucose 6-phosphate. | + | [https://www.uniprot.org/uniprot/GLK_ECO57 GLK_ECO57] Not highly important in E.coli as glucose is transported into the cell by the PTS system already as glucose 6-phosphate. |
| | == 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: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: Glucokinase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cygler, M]] | + | [[Category: Cygler M]] |
| - | [[Category: Iannuzzi, P]] | + | [[Category: Iannuzzi P]] |
| - | [[Category: Li, Y]] | + | [[Category: Li Y]] |
| - | [[Category: Lunin, V V]] | + | [[Category: Lunin VV]] |
| - | [[Category: Matte, A]] | + | [[Category: Matte A]] |
| - | [[Category: Schrag, J D]] | + | [[Category: Schrag JD]] |
| - | [[Category: Atp-dependent]]
| + | |
| - | [[Category: Glucose binding]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
GLK_ECO57 Not highly important in E.coli as glucose is transported into the cell by the PTS system already as glucose 6-phosphate.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Intracellular glucose in Escherichia coli cells imported by phosphoenolpyruvate-dependent phosphotransferase system-independent uptake is phosphorylated by glucokinase by using ATP to yield glucose-6-phosphate. Glucokinases (EC 2.7.1.2) are functionally distinct from hexokinases (EC 2.7.1.1) with respect to their narrow specificity for glucose as a substrate. While structural information is available for ADP-dependent glucokinases from Archaea, no structural information exists for the large sequence family of eubacterial ATP-dependent glucokinases. Here we report the first structure determination of a microbial ATP-dependent glucokinase, that from E. coli O157:H7. The crystal structure of E. coli glucokinase has been determined to a 2.3-A resolution (apo form) and refined to final Rwork/Rfree factors of 0.200/0.271 and to 2.2-A resolution (glucose complex) with final Rwork/Rfree factors of 0.193/0.265. E. coli GlK is a homodimer of 321 amino acid residues. Each monomer folds into two domains, a small alpha/beta domain (residues 2 to 110 and 301 to 321) and a larger alpha+beta domain (residues 111 to 300). The active site is situated in a deep cleft between the two domains. E. coli GlK is structurally similar to Saccharomyces cerevisiae hexokinase and human brain hexokinase I but is distinct from the ADP-dependent GlKs. Bound glucose forms hydrogen bonds with the residues Asn99, Asp100, Glu157, His160, and Glu187, all of which, except His160, are structurally conserved in human hexokinase 1. Glucose binding results in a closure of the small domains, with a maximal Calpha shift of approximately 10 A. A catalytic mechanism is proposed that is consistent with Asp100 functioning as the general base, abstracting a proton from the O6 hydroxyl of glucose, followed by nucleophilic attack at the gamma-phosphoryl group of ATP, yielding glucose-6-phosphate as the product.
Crystal structures of Escherichia coli ATP-dependent glucokinase and its complex with glucose.,Lunin VV, Li Y, Schrag JD, Iannuzzi P, Cygler M, Matte A J Bacteriol. 2004 Oct;186(20):6915-27. PMID:15466045[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lunin VV, Li Y, Schrag JD, Iannuzzi P, Cygler M, Matte A. Crystal structures of Escherichia coli ATP-dependent glucokinase and its complex with glucose. J Bacteriol. 2004 Oct;186(20):6915-27. PMID:15466045 doi:186/20/6915
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