2jg1
From Proteopedia
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|PDB= 2jg1 |SIZE=350|CAPTION= <scene name='initialview01'>2jg1</scene>, resolution 2.00Å | |PDB= 2jg1 |SIZE=350|CAPTION= <scene name='initialview01'>2jg1</scene>, resolution 2.00Å | ||
|SITE= <scene name='pdbsite=AC1:Anp+Binding+Site+For+Chain+D'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Anp+Binding+Site+For+Chain+D'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=TA6:TAGATOSE-6-PHOSPHATE'>TA6</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Tagatose-6-phosphate_kinase Tagatose-6-phosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.144 2.7.1.144] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Tagatose-6-phosphate_kinase Tagatose-6-phosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.144 2.7.1.144] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jg1 OCA], [http://www.ebi.ac.uk/pdbsum/2jg1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2jg1 RCSB]</span> | ||
}} | }} | ||
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[[Category: Mcsweeney, S M.]] | [[Category: Mcsweeney, S M.]] | ||
[[Category: Miallau, L.]] | [[Category: Miallau, L.]] | ||
| - | [[Category: ANP]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: TA6]] | ||
[[Category: conformational change]] | [[Category: conformational change]] | ||
[[Category: d-tagatose-6-phosphate kinase]] | [[Category: d-tagatose-6-phosphate kinase]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''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 03:57:42 2008'' |
Revision as of 00:57, 31 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , | ||||||
| Activity: | Tagatose-6-phosphate kinase, with EC number 2.7.1.144 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF STAPHYLOCOCCUS AUREUS D-TAGATOSE-6-PHOSPHATE KINASE WITH COFACTOR AND SUBSTRATE
Overview
High resolution structures of Staphylococcus aureus d-tagatose-6-phosphate kinase (LacC) in two crystal forms are herein reported. The structures define LacC in apoform, in binary complexes with ADP or the co-factor analogue AMP-PNP, and in a ternary complex with AMP-PNP and D-tagatose-6-phosphate. The tertiary structure of the LacC monomer, which is closely related to other members of the pfkB subfamily of carbohydrate kinases, is composed of a large alpha/beta core domain and a smaller, largely beta "lid." Four extended polypeptide segments connect these two domains. Dimerization of LacC occurs via interactions between lid domains, which come together to form a beta-clasp structure. Residues from both subunits contribute to substrate binding. LacC adopts a closed structure required for phosphoryl transfer only when both substrate and co-factor are bound. A reaction mechanism similar to that used by other phosphoryl transferases is proposed, although unusually, when both substrate and co-factor are bound to the enzyme two Mg(2+) ions are observed in the active site. A new motif of amino acid sequence conservation common to the pfkB subfamily of carbohydrate kinases is identified.
About this Structure
2JG1 is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
Structures of Staphylococcus aureus D-tagatose-6-phosphate kinase implicate domain motions in specificity and mechanism., Miallau L, Hunter WN, McSweeney SM, Leonard GA, J Biol Chem. 2007 Jul 6;282(27):19948-57. Epub 2007 Apr 25. PMID:17459874
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