1vrp: Difference between revisions
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|PDB= 1vrp |SIZE=350|CAPTION= <scene name='initialview01'>1vrp</scene>, resolution 2.1Å | |PDB= 1vrp |SIZE=350|CAPTION= <scene name='initialview01'>1vrp</scene>, resolution 2.1Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=IOM:(DIAMINOMETHYL-METHYL-AMINO)-ACETIC+ACID'>IOM</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Creatine_kinase Creatine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.2 2.7.3.2] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Creatine_kinase Creatine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.2 2.7.3.2] </span> | ||
|GENE= FSCCKPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7787 Torpedo californica]) | |GENE= FSCCKPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7787 Torpedo californica]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1qh4|1QH4]], [[1bg0|1BG0]], [[2crk|2CRK]], [[1g0w|1G0W]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vrp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vrp OCA], [http://www.ebi.ac.uk/pdbsum/1vrp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vrp RCSB]</span> | |||
}} | }} | ||
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[[Category: McLeish, M J.]] | [[Category: McLeish, M J.]] | ||
[[Category: Wang, P F.]] | [[Category: Wang, P F.]] | ||
[[Category: arginine kinase]] | [[Category: arginine kinase]] | ||
[[Category: creatine kinase]] | [[Category: creatine kinase]] | ||
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[[Category: transition-state analogue complex]] | [[Category: transition-state analogue complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:27:45 2008'' | ||
Revision as of 00:27, 31 March 2008
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| , resolution 2.1Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Gene: | FSCCKPA (Torpedo californica) | ||||||
| Activity: | Creatine kinase, with EC number 2.7.3.2 | ||||||
| Related: | 1QH4, 1BG0, 2CRK, 1G0W
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The 2.1 Structure of T. californica Creatine Kinase Complexed with the Transition-State Analogue Complex, ADP-Mg 2+ /NO3-/Creatine
OverviewOverview
Creatine kinase (CK) catalyzes the reversible conversion of creatine and ATP to phosphocreatine and ADP, thereby helping maintain energy homeostasis in the cell. Here we report the first X-ray structure of CK bound to a transition-state analogue complex (CK-TSAC). Cocrystallization of the enzyme from Torpedo californica (TcCK) with ADP-Mg(2+), nitrate, and creatine yielded a homodimer, one monomer of which was liganded to a TSAC complex while the second monomer was bound to ADP-Mg(2+) alone. The structures of both monomers were determined to 2.1 A resolution. The creatine is located with the guanidino nitrogen cis to the methyl group positioned to perform in-line attack at the gamma-phosphate of ATP-Mg(2+), while the ADP-Mg(2+) is in a conformation similar to that found in the TSAC-bound structure of the homologue arginine kinase (AK). Three ligands to Mg(2+) are contributed by ADP and nitrate and three by ordered water molecules. The most striking difference between the substrate-bound and TSAC-bound structures is the movement of two loops, comprising residues 60-70 and residues 323-332. In the TSAC-bound structure, both loops move into the active site, resulting in the positioning of two hydrophobic residues (one from each loop), Ile69 and Val325, near the methyl group of creatine. This apparently provides a specificity pocket for optimal creatine binding as this interaction is missing in the AK structure. In addition, the active site of the transition-state analogue complex is completely occluded from solvent, unlike the ADP-Mg(2+)-bound monomer and the unliganded structures reported previously.
About this StructureAbout this Structure
1VRP is a Single protein structure of sequence from Torpedo californica. This structure supersedes the now removed PDB entry 1N16. Full crystallographic information is available from OCA.
ReferenceReference
The 2.1 A structure of Torpedo californica creatine kinase complexed with the ADP-Mg(2+)-NO(3)(-)-creatine transition-state analogue complex., Lahiri SD, Wang PF, Babbitt PC, McLeish MJ, Kenyon GL, Allen KN, Biochemistry. 2002 Nov 26;41(47):13861-7. PMID:12437342
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