2j41

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[[Image:2j41.jpg|left|200px]]
 
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==Crystal structure of Staphylococcus aureus guanylate monophosphate kinase==
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The line below this paragraph, containing "STRUCTURE_2j41", creates the "Structure Box" on the page.
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<StructureSection load='2j41' size='340' side='right'caption='[[2j41]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2j41]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J41 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J41 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5GP:GUANOSINE-5-MONOPHOSPHATE'>5GP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_2j41| PDB=2j41 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2j41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j41 OCA], [https://pdbe.org/2j41 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j41 RCSB], [https://www.ebi.ac.uk/pdbsum/2j41 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j41 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/KGUA_STAAC KGUA_STAAC] Essential for recycling GMP and indirectly, cGMP (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j4/2j41_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2j41 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''CRYSTAL STRUCTURE OF STAPHYLOCOCCUS AUREUS GUANYLATE MONOPHOSPHATE KINASE'''
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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<ref>PMID:17012781</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2j41" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Guanylate kinase 3D structures|Guanylate kinase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2J41 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J41 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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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://www.ncbi.nlm.nih.gov/pubmed/17012781 17012781]
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[[Category: Guanylate kinase]]
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[[Category: Single protein]]
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[[Category: Staphylococcus aureus]]
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[[Category: Charles, I.]]
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[[Category: Dhaliwal, B.]]
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[[Category: Hawkins, A R.]]
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[[Category: Lockyer, M.]]
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[[Category: Omari, K El.]]
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[[Category: Stammers, D K.]]
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[[Category: Atp-binding]]
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[[Category: Gmk]]
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[[Category: Gmp]]
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[[Category: Kinase]]
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[[Category: Nucleotide-binding]]
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[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
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[[Category: Transferase]]
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[[Category: Charles I]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:18:05 2008''
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[[Category: Dhaliwal B]]
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[[Category: El Omari K]]
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[[Category: Hawkins AR]]
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[[Category: Lockyer M]]
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[[Category: Stammers DK]]

Current revision

Crystal structure of Staphylococcus aureus guanylate monophosphate kinase

PDB ID 2j41

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