2j41
From Proteopedia
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| - | [[Image:2j41.jpg|left|200px]]<br /><applet load="2j41" size=" | + | [[Image:2j41.jpg|left|200px]]<br /><applet load="2j41" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2j41, resolution 1.90Å" /> | caption="2j41, resolution 1.90Å" /> | ||
'''CRYSTAL STRUCTURE OF STAPHYLOCOCCUS AUREUS GUANYLATE MONOPHOSPHATE KINASE'''<br /> | '''CRYSTAL STRUCTURE OF STAPHYLOCOCCUS AUREUS GUANYLATE MONOPHOSPHATE KINASE'''<br /> | ||
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| + | ==Overview== | ||
| + | Nucleotide monophosphate kinases (NMPKs) are potential antimicrobial drug, targets owing to their role in supplying DNA and RNA precursors. The, present work reports the crystal structure of Staphylococcus aureus, guanylate monophosphate kinase (SaGMK) at 1.9 A resolution. The structure, shows that unlike most GMKs SaGMK is dimeric, confirming the role of the, extended C-terminus in dimer formation as first observed for Escherichia, coli GMK (EcGMK). One of the two SaGMK dimers within the crystal, asymmetric unit has two monomers in different conformations: an open form, with a bound sulfate ion (mimicking the beta-phosphate of ATP) and a, closed form with bound GMP and sulfate ion. GMP-induced domain movements, in SaGMK can thus be defined by comparison of these conformational states., Like other GMKs, the binding of GMP firstly triggers a partial closure of, the enzyme, diminishing the distance between the GMP-binding and, ATP-binding sites. In addition, the closed structure shows the presence of, a potassium ion in contact with the guanine ring of GMP. The potassium ion, appears to form an integral part of the GMP-binding site, as the Tyr36, side chain has significantly moved to form a metal ion-ligand coordination, involving the lone pair of the side-chain O atom. The potassium-binding, site might also be exploited in the design of novel inhibitors. | ||
==About this Structure== | ==About this Structure== | ||
| - | 2J41 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with SO4, K and 5GP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Guanylate_kinase Guanylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.8 2.7.4.8] Known structural/functional | + | 2J41 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=K:'>K</scene> and <scene name='pdbligand=5GP:'>5GP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Guanylate_kinase Guanylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.8 2.7.4.8] Known structural/functional Sites: <scene name='pdbsite=AC1:So4 Binding Site For Residue C 1198'>AC1</scene>, <scene name='pdbsite=AC2:So4 Binding Site For Residue B 1206'>AC2</scene>, <scene name='pdbsite=AC3:So4 Binding Site For Residue D 1207'>AC3</scene>, <scene name='pdbsite=AC4:So4 Binding Site For Residue A 1198'>AC4</scene>, <scene name='pdbsite=AC5:So4 Binding Site For Residue D 1208'>AC5</scene>, <scene name='pdbsite=AC6:K Binding Site For Residue B 1207'>AC6</scene>, <scene name='pdbsite=AC7:K Binding Site For Residue C 1199'>AC7</scene>, <scene name='pdbsite=AC8:K Binding Site For Residue D 1209'>AC8</scene>, <scene name='pdbsite=AC9:5gp Binding Site For Residue C 1200'>AC9</scene>, <scene name='pdbsite=BC1:5gp Binding Site For Residue D 1210'>BC1</scene> and <scene name='pdbsite=BC2:5gp Binding Site For Residue B 1208'>BC2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J41 OCA]. |
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| + | ==Reference== | ||
| + | Structure of Staphylococcus aureus guanylate monophosphate kinase., El Omari K, Dhaliwal B, Lockyer M, Charles I, Hawkins AR, Stammers DK, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Oct 1;62(Pt, 10):949-53. Epub 2006 Sep 19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17012781 17012781] | ||
[[Category: Guanylate kinase]] | [[Category: Guanylate kinase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jan 31 10:57:18 2008'' |
Revision as of 08:57, 31 January 2008
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CRYSTAL STRUCTURE OF STAPHYLOCOCCUS AUREUS GUANYLATE MONOPHOSPHATE KINASE
Overview
Nucleotide monophosphate kinases (NMPKs) are potential antimicrobial drug, targets owing to their role in supplying DNA and RNA precursors. The, present work reports the crystal structure of Staphylococcus aureus, guanylate monophosphate kinase (SaGMK) at 1.9 A resolution. The structure, shows that unlike most GMKs SaGMK is dimeric, confirming the role of the, extended C-terminus in dimer formation as first observed for Escherichia, coli GMK (EcGMK). One of the two SaGMK dimers within the crystal, asymmetric unit has two monomers in different conformations: an open form, with a bound sulfate ion (mimicking the beta-phosphate of ATP) and a, closed form with bound GMP and sulfate ion. GMP-induced domain movements, in SaGMK can thus be defined by comparison of these conformational states., Like other GMKs, the binding of GMP firstly triggers a partial closure of, the enzyme, diminishing the distance between the GMP-binding and, ATP-binding sites. In addition, the closed structure shows the presence of, a potassium ion in contact with the guanine ring of GMP. The potassium ion, appears to form an integral part of the GMP-binding site, as the Tyr36, side chain has significantly moved to form a metal ion-ligand coordination, involving the lone pair of the side-chain O atom. The potassium-binding, site might also be exploited in the design of novel inhibitors.
About this Structure
2J41 is a Single protein structure of sequence from Staphylococcus aureus with , and as ligands. Active as Guanylate kinase, with EC number 2.7.4.8 Known structural/functional Sites: , , , , , , , , , and . Full crystallographic information is available from OCA.
Reference
Structure of Staphylococcus aureus guanylate monophosphate kinase., El Omari K, Dhaliwal B, Lockyer M, Charles I, Hawkins AR, Stammers DK, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Oct 1;62(Pt, 10):949-53. Epub 2006 Sep 19. PMID:17012781
Page seeded by OCA on Thu Jan 31 10:57:18 2008
Categories: Guanylate kinase | Single protein | Staphylococcus aureus | Charles, I. | Dhaliwal, B. | Hawkins, A.R. | Lockyer, M. | Omari, K.El. | Stammers, D.K. | 5GP | K | SO4 | Atp-binding | Gmk | Gmp | Kinase | Nucleotide-binding | Transferase
