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1gmp

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[[Image:1gmp.jpg|left|200px]]
 
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==COMPLEX OF RIBONUCLEASE FROM STREPTOMYCES AUREOFACIENS WITH 2'-GMP AT 1.7 ANGSTROMS RESOLUTION==
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The line below this paragraph, containing "STRUCTURE_1gmp", creates the "Structure Box" on the page.
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<StructureSection load='1gmp' size='340' side='right'caption='[[1gmp]], [[Resolution|resolution]] 1.70&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'>[[1gmp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Kitasatospora_aureofaciens Kitasatospora aureofaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GMP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GMP 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]] 1.7&#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=2GP:GUANOSINE-2-MONOPHOSPHATE'>2GP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_1gmp| PDB=1gmp | 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=1gmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gmp OCA], [https://pdbe.org/1gmp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gmp RCSB], [https://www.ebi.ac.uk/pdbsum/1gmp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gmp ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RNSA_KITAU RNSA_KITAU]
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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/gm/1gmp_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1gmp ConSurf].
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<div style="clear:both"></div>
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'''COMPLEX OF RIBONUCLEASE FROM STREPTOMYCES AUREOFACIENS WITH 2'-GMP AT 1.7 ANGSTROMS RESOLUTION'''
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==See Also==
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*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The crystal structure of a complex of ribonuclease from Streptomyces aureofaciens (RNase Sa) with guanosine-2'-monophosphate (2'-GMP) has been refined against synchrotron data recorded from a single crystal using radiation from beamline X31 at EMBL, Hamburg, and an imaging plate scanner. The crystals are in space group P2(1)2(1)2(1) with cell dimensions a = 64.7, b = 78.8 and c = 39.1 A. The structure has two enzyme molecules in the asymmetric unit, complexed with 2'-GMP inhibitor with occupancies of 1 and 2/3 (different to the 3'-GMP complex crystal structure where only one of the two independent RNase Sa molecules binds nucleotide), 492 associated water molecules and one sulfate ion, and was refined using all data between 10.0 and 1.7 A to a final crystallographic R factor of 13.25%. Binding of the base to the enzyme confirms the basis for the guanine specificity but the structural results still do not provide direct evidence of the identity and role of the particular residues involved in the catalytic process. New native RNase Sa data to 1.8 A were recorded to provide a reference set measured under comparable experimental conditions. The crystals are in the same space group and have the same lattice as those of the 2'-GMP complex. The native structure with 423 water molecules was refined in a similar manner to the complex to a final R factor of 13.87%. 1.77 A resolution data were independently measured on a 2'-GMP complex crystal at UCLA using an R-AXIS II image plate scanner mounted on a conventional source. The cell dimensions were essentially the same as above. 2'-GMP was bound more fully to molecule A than to molecule B of the RNase Sa. The structure was refined to an R factor of 14.64% with 388 water molecules. This work follows on from the structure determination of native RNase Sa and its complex with 3'-GMP [Sevcik, Dodson &amp; Dodson (1991). Acta Cryst. B47, 240-253].
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[[Category: Kitasatospora aureofaciens]]
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[[Category: Large Structures]]
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==About this Structure==
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[[Category: Dauter Z]]
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1GMP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_aureofaciens Streptomyces aureofaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GMP OCA].
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[[Category: Hill C]]
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[[Category: Sevcik J]]
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==Reference==
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[[Category: Wilson K]]
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Complex of ribonuclease from Streptomyces aureofaciens with 2'-GMP at 1.7 A resolution., Sevcik J, Hill CP, Dauter Z, Wilson KS, Acta Crystallogr D Biol Crystallogr. 1993 Mar 1;49(Pt 2):257-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299531 15299531]
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[[Category: Single protein]]
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[[Category: Streptomyces aureofaciens]]
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[[Category: Dauter, Z.]]
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[[Category: Hill, C.]]
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[[Category: Sevcik, J.]]
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[[Category: Wilson, K.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:45:30 2008''
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Current revision

COMPLEX OF RIBONUCLEASE FROM STREPTOMYCES AUREOFACIENS WITH 2'-GMP AT 1.7 ANGSTROMS RESOLUTION

PDB ID 1gmp

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