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| <StructureSection load='4am1' size='340' side='right'caption='[[4am1]], [[Resolution|resolution]] 1.25Å' scene=''> | | <StructureSection load='4am1' size='340' side='right'caption='[[4am1]], [[Resolution|resolution]] 1.25Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[4am1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Litopenaeus_vannamei Litopenaeus vannamei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AM1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AM1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4am1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Penaeus_vannamei Penaeus vannamei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AM1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AM1 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/Arginine_kinase Arginine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.3 2.7.3.3] </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]] 1.25Å</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=4am1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4am1 OCA], [http://pdbe.org/4am1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4am1 RCSB], [http://www.ebi.ac.uk/pdbsum/4am1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4am1 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=4am1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4am1 OCA], [https://pdbe.org/4am1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4am1 RCSB], [https://www.ebi.ac.uk/pdbsum/4am1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4am1 ProSAT]</span></td></tr> |
| </table> | | </table> |
- | <div style="background-color:#fffaf0;">
| + | == Function == |
- | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/KARG0_PENVA KARG0_PENVA] Catalyzes the reversible transfer of high energy ATP gamma-phosphate group to L-arginine (PubMed:17496423, PubMed:27072556, PubMed:22750864, PubMed:23873077). Has nucleoside diphosphate kinase-like activity toward dTDP. Binds and phosphorylates dTDP using ATP as a phosphate donor. Does not phosphorylate dADP, dCDP, dGDP, dTMP or thymidine (PubMed:27072556).<ref>PMID:17496423</ref> <ref>PMID:22750864</ref> <ref>PMID:23873077</ref> <ref>PMID:27072556</ref> |
- | Crystals of an unligated monomeric arginine kinase from the Pacific whiteleg shrimp Litopenaeus vannamei (LvAK) were successfully obtained using the microbatch method. Crystallization conditions and preliminary X-ray diffraction analysis to 1.25 A resolution are reported. Data were collected at 100 K on NSLS beamline X6A. The crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 56.5, b = 70.2, c = 81.7 A. One monomer per asymmetric unit was found, with a Matthews coefficient (V(M)) of 2.05 A(3) Da(-1) and 40% solvent content. Initial phases were determined by molecular replacement using a homology model of LvAK as the search model. Refinement was performed with PHENIX, with final R(work) and R(free) values of 0.15 and 0.19, respectively. Biological analysis of the structure is currently in progress.
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- | | + | |
- | Crystallization and X-ray diffraction studies of arginine kinase from the white Pacific shrimp Litopenaeus vannamei.,Lopez-Zavala AA, Sotelo-Mundo RR, Garcia-Orozco KD, Isac-Martinez F, Brieba LG, Rudino-Pinera E Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jul 1;68(Pt 7):783-5. Epub, 2012 Jun 27. PMID:22750864<ref>PMID:22750864</ref>
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- | | + | |
- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
- | </div> | + | |
- | <div class="pdbe-citations 4am1" style="background-color:#fffaf0;"></div> | + | |
| | | |
| ==See Also== | | ==See Also== |
- | *[[Arginine kinase|Arginine kinase]] | + | *[[Arginine kinase 3D structures|Arginine kinase 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Arginine kinase]] | + | [[Category: Large Structures]] |
- | [[Category: Litopenaeus vannamei]] | + | [[Category: Penaeus vannamei]] |
- | [[Category: Brieba, L G]] | + | [[Category: Brieba LG]] |
- | [[Category: Garcia-Orozco, K D]] | + | [[Category: Garcia-Orozco KD]] |
- | [[Category: Isac-Martinez, F]] | + | [[Category: Isac-Martinez F]] |
- | [[Category: Lopez-Zavala, A A]] | + | [[Category: Lopez-Zavala AA]] |
- | [[Category: Rudino-Pinera, E]] | + | [[Category: Rudino-Pinera E]] |
- | [[Category: Sotelo-Mundo, R R]] | + | [[Category: Sotelo-Mundo RR]] |
- | [[Category: Transferase]]
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| Structural highlights
Function
KARG0_PENVA Catalyzes the reversible transfer of high energy ATP gamma-phosphate group to L-arginine (PubMed:17496423, PubMed:27072556, PubMed:22750864, PubMed:23873077). Has nucleoside diphosphate kinase-like activity toward dTDP. Binds and phosphorylates dTDP using ATP as a phosphate donor. Does not phosphorylate dADP, dCDP, dGDP, dTMP or thymidine (PubMed:27072556).[1] [2] [3] [4]
See Also
References
- ↑ García-Orozco KD, Aispuro-Hernández E, Yepiz-Plascencia G, Calderón-de-la-Barca AM, Sotelo-Mundo RR. Molecular characterization of arginine kinase, an allergen from the shrimp Litopenaeus vannamei. Int Arch Allergy Immunol. 2007;144(1):23-8. PMID:17496423 doi:10.1159/000102610
- ↑ Lopez-Zavala AA, Sotelo-Mundo RR, Garcia-Orozco KD, Isac-Martinez F, Brieba LG, Rudino-Pinera E. Crystallization and X-ray diffraction studies of arginine kinase from the white Pacific shrimp Litopenaeus vannamei. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jul 1;68(Pt 7):783-5. Epub, 2012 Jun 27. PMID:22750864 doi:10.1107/S1744309112020180
- ↑ Lopez-Zavala AA, Garcia-Orozco KD, Carrasco-Miranda JS, Sugich-Miranda R, Velazquez-Contreras EF, Criscitiello MF, Brieba LG, Rudino-Pinera E, Sotelo-Mundo RR. Crystal structure of shrimp arginine kinase in binary complex with arginine-a molecular view of the phosphagen precursor binding to the enzyme. J Bioenerg Biomembr. 2013 Jul 20. PMID:23873077 doi:10.1007/s10863-013-9521-0
- ↑ Lopez-Zavala AA, Sotelo-Mundo RR, Hernandez-Flores JM, Lugo-Sanchez ME, Sugich-Miranda R, Garcia-Orozco KD. Arginine kinase shows nucleoside diphosphate kinase-like activity toward deoxythymidine diphosphate. J Bioenerg Biomembr. 2016 Jun;48(3):301-8. PMID:27072556 doi:10.1007/s10863-016-9660-1
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