1gin: Difference between revisions

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[[Image:1gin.gif|left|200px]]<br />
<applet load="1gin" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1gin, resolution 2.8&Aring;" />
'''CRYSTAL STRUCTURE OF ADENYLOSUCCINATE SYNTHETASE FROM ESCHERICHIA COLI COMPLEXED WITH GDP, IMP, HADACIDIN, NO3-, AND MG2+. DATA COLLECTED AT 298K (PH 6.5).'''<br />


==Overview==
==CRYSTAL STRUCTURE OF ADENYLOSUCCINATE SYNTHETASE FROM ESCHERICHIA COLI COMPLEXED WITH GDP, IMP, HADACIDIN, NO3-, AND MG2+. DATA COLLECTED AT 298K (PH 6.5).==
Crystal structures of adenylosuccinate synthetase from Esherichia coli, complexed with Mg2+, IMP, GDP, NO3- and hadacidin at 298 and 100 K have, been refined to R-factors of 0.188 and 0.206 against data to 2.8 A and 2.5, A resolution, respectively. Conformational changes of up to 9 A relative, to the unligated enzyme occur in loops that bind to Mg2+, GDP, IMP and, hadacidin. Mg2+ binds directly to GDP, NO3-, hadacidin and the protein, but is only five-coordinated. Asp13, which approaches, but does not occupy, the sixth coordination site of Mg2+, hydrogen bonds to N1 of IMP. The, nitrogen atom of NO3- is approximately 2.7 A from O6 of IMP, reflecting a, strong electrostatic interaction between the electron-deficient nitrogen, atom and the electron-rich O6. The spatial relationships between ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9000627 (full description)]]
<StructureSection load='1gin' size='340' side='right'caption='[[1gin]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1gin]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GIN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GIN FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=HDA:HADACIDIN'>HDA</scene>, <scene name='pdbligand=IMP:INOSINIC+ACID'>IMP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gin FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gin OCA], [https://pdbe.org/1gin PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gin RCSB], [https://www.ebi.ac.uk/pdbsum/1gin PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gin ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PURA_ECOLI PURA_ECOLI] Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity).[HAMAP-Rule:MF_00011]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gi/1gin_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1gin ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1GIN is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with MG, NO3, HAD, IMP and GDP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Adenylosuccinate_synthase Adenylosuccinate synthase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.4 6.3.4.4]]. Structure known Active Sites: ASP, GNS and IMP. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GIN OCA]].
*[[Adenylosuccinate synthetase 3D structures|Adenylosuccinate synthetase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structures of adenylosuccinate synthetase from Escherichia coli complexed with GDP, IMP hadacidin, NO3-, and Mg2+., Poland BW, Fromm HJ, Honzatko RB, J Mol Biol. 1996 Dec 20;264(5):1013-27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9000627 9000627]
[[Category: Adenylosuccinate synthase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Fromm, H.J.]]
[[Category: Fromm HJ]]
[[Category: Honzatko, R.B.]]
[[Category: Honzatko RB]]
[[Category: Poland, B.W.]]
[[Category: Poland BW]]
[[Category: GDP]]
[[Category: HAD]]
[[Category: IMP]]
[[Category: MG]]
[[Category: NO3]]
[[Category: gtp-hydrolyzing enzymes]]
[[Category: ligase]]
[[Category: purine nucleotide biosynthesis]]
 
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Retrieved from "https://proteopedia.org/1gin"