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| | <StructureSection load='1f3x' size='340' side='right'caption='[[1f3x]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='1f3x' size='340' side='right'caption='[[1f3x]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1f3x]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F3X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F3X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1f3x]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F3X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F3X FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</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]] 2.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1f3w|1f3w]], [[1pkn|1pkn]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Pyruvate_kinase Pyruvate kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.40 2.7.1.40] </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=1f3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f3x OCA], [https://pdbe.org/1f3x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f3x RCSB], [https://www.ebi.ac.uk/pdbsum/1f3x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f3x 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=1f3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f3x OCA], [https://pdbe.org/1f3x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f3x RCSB], [https://www.ebi.ac.uk/pdbsum/1f3x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f3x ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/KPYM_RABIT KPYM_RABIT]] Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation (By similarity).
| + | [https://www.uniprot.org/uniprot/KPYM_RABIT KPYM_RABIT] Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation (By similarity). |
| | == 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: European rabbit]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pyruvate kinase]] | + | [[Category: Oryctolagus cuniculus]] |
| - | [[Category: Czerwinski, E W]] | + | [[Category: Czerwinski EW]] |
| - | [[Category: Fox, R O]] | + | [[Category: Fox RO]] |
| - | [[Category: Friesen, R H.E]] | + | [[Category: Friesen RHE]] |
| - | [[Category: Lee, J C]] | + | [[Category: Lee JC]] |
| - | [[Category: Watowich, S J]] | + | [[Category: Watowich SJ]] |
| - | [[Category: White, M A]] | + | [[Category: White MA]] |
| - | [[Category: Wooll, J O]] | + | [[Category: Wooll JO]] |
| - | [[Category: Muscle isozyme]]
| + | |
| - | [[Category: S402p]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
KPYM_RABIT Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation (By similarity).
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
Mammalian pyruvate kinase (PK) is a four-domain enzyme that is active as a homo-tetramer. Tissue-specific isozymes of PK exhibit distinct levels of allosteric regulation. PK expressed in muscle tissue (M1-PK) shows hyperbolic steady-state kinetics, whereas PK expressed in kidney tissue (M2-PK) displays sigmoidal kinetics. Rabbit M1 and M2-PK are isozymes whose sequences differ in only 22 out of 530 residues per subunit, and these changes are localized in an inter-subunit interface. Previous studies have shown that a single amino acid mutation to M1-PK at either the Y (S402P) or Z (T340 M) subunit interface can confer a level of allosteric regulation that is intermediate to M1-PK and M2-PK. In an effort to elucidate the roles of the inter-subunit interaction in signal transmission and the functional/structural connectivity between these interfaces, the S402P mutant of M1-PK was crystallized and its structure resolved to 2.8 A. Although the overall S402P M1-PK structure is nearly identical with the wild-type structure within experimental error, significant differences in the conformation of the backbone are found at the site of mutation along the Y interface. In addition, there is a significant change along the Z interface, namely, a loss of an inter-subunit salt-bridge between Asp177 of domain B and Arg341 of domain A of the opposing subunit. Concurrent with the loss of the salt-bridge is an increase in the degree of rotational flexibility of domain B that constitutes the active site. Comparison of previous PK structures shows a correlation between an increase in this domain movement with the loss of the Asp177: Arg341 salt-bridge. These results identify the structural linkages between the Y and Z interfaces in regulating the interconversion of conformational states of rabbit M1-PK.
Structural and functional linkages between subunit interfaces in mammalian pyruvate kinase.,Wooll JO, Friesen RH, White MA, Watowich SJ, Fox RO, Lee JC, Czerwinski EW J Mol Biol. 2001 Sep 21;312(3):525-40. PMID:11563914[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wooll JO, Friesen RH, White MA, Watowich SJ, Fox RO, Lee JC, Czerwinski EW. Structural and functional linkages between subunit interfaces in mammalian pyruvate kinase. J Mol Biol. 2001 Sep 21;312(3):525-40. PMID:11563914 doi:10.1006/jmbi.2001.4978
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