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| | <StructureSection load='2zci' size='340' side='right'caption='[[2zci]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='2zci' size='340' side='right'caption='[[2zci]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2zci]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZCI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2ZCI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2zci]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZCI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZCI FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoenolpyruvate_carboxykinase_(GTP) Phosphoenolpyruvate carboxykinase (GTP)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.32 4.1.1.32] </span></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]] 2.3Å</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=2zci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zci OCA], [http://pdbe.org/2zci PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zci RCSB], [http://www.ebi.ac.uk/pdbsum/2zci PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zci ProSAT]</span></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=2zci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zci OCA], [https://pdbe.org/2zci PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zci RCSB], [https://www.ebi.ac.uk/pdbsum/2zci PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zci ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PCKG_CORGL PCKG_CORGL]] Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.<ref>PMID:11565516</ref> | + | [https://www.uniprot.org/uniprot/PCKG_CORGL PCKG_CORGL] Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.<ref>PMID:11565516</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: Corynebacterium glutamicum]] | | [[Category: Corynebacterium glutamicum]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Aich, S]] | + | [[Category: Aich S]] |
| - | [[Category: Delbaere, L T.J]] | + | [[Category: Delbaere LTJ]] |
| - | [[Category: Prasad, L]] | + | [[Category: Prasad L]] |
| - | [[Category: Carboxykinase]]
| + | |
| - | [[Category: Gtp-dependent]]
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| - | [[Category: Lyase]]
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| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
Function
PCKG_CORGL Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.[1]
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
GTP-dependent phosphoenolpyruvate carboxykinase (PCK) is the key enzyme that controls the blood glucose level during fasting in higher animals. Here we report the first substrate-free structure of a GTP-dependent phosphoenolpyruvate (PEP) carboxykinase from a bacterium, Corynebacterium glutamicum (CgPCK). The protein crystallizes in space group P2(1) with four molecules per asymmetric unit. The 2.3A resolution structure was solved by molecular replacement using the human cytosolic PCK (hcPCK) structure (PDB ID: 1KHF) as the starting model. The four molecules in the asymmetric unit pack as two dimers, and is an artifact of crystal packing. However, the P-loop and the guanine binding loop of the substrate-free CgPCK structure have different conformations from the other published GTP-specific PCK structures, which all have bound substrates and/or metal ions. It appears that a change in the P-loop and guanine binding loop conformation is necessary for substrate binding in GTP-specific PCKs, as opposed to overall domain movement in ATP-specific PCKs.
Structure of a GTP-dependent bacterial PEP-carboxykinase from Corynebacterium glutamicum.,Aich S, Prasad L, Delbaere LT Int J Biochem Cell Biol. 2008;40(8):1597-603. Epub 2007 Dec 23. PMID:18234538[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Riedel C, Rittmann D, Dangel P, Mockel B, Petersen S, Sahm H, Eikmanns BJ. Characterization of the phosphoenolpyruvate carboxykinase gene from Corynebacterium glutamicum and significance of the enzyme for growth and amino acid production. J Mol Microbiol Biotechnol. 2001 Oct;3(4):573-83. PMID:11565516
- ↑ Aich S, Prasad L, Delbaere LT. Structure of a GTP-dependent bacterial PEP-carboxykinase from Corynebacterium glutamicum. Int J Biochem Cell Biol. 2008;40(8):1597-603. Epub 2007 Dec 23. PMID:18234538 doi:10.1016/j.biocel.2007.12.002
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