1kkf

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(New page: 200px<br /><applet load="1kkf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kkf, resolution 2.6&Aring;" /> '''Complex of E. coli Ad...)
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[[Image:1kkf.gif|left|200px]]<br /><applet load="1kkf" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1kkf, resolution 2.6&Aring;" />
 
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'''Complex of E. coli Adenylosuccinate Synthetase with IMP, Hadacidin, Pyrophosphate, and Mg'''<br />
 
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==Overview==
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==Complex of E. coli Adenylosuccinate Synthetase with IMP, Hadacidin, Pyrophosphate, and Mg==
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A complete set of substrate/substrate analogs of adenylosuccinate, synthetase from Escherichia coli induces dimer formation and a transition, from a disordered to an ordered active site. The most striking of the, ligand-induced effects is the movement of loop 40-53 by up to 9 A. Crystal, structures of the partially ligated synthetase, which either combine IMP, and hadacidin or IMP, hadacidin, and Mg(2+)-pyrophosphate, have ordered, active sites, comparable with the fully ligated enzyme. More, significantly, a crystal structure of the synthetase with IMP alone, exhibits a largely ordered active site, which includes the 9 A movement of, loop 40-53 but does not include conformational adjustments to backbone, carbonyl 40 (Mg(2+) interaction element) and loop 298-304 (L-aspartate, binding element). Interactions involving the 5'-phosphoryl group of IMP, evidently trigger the formation of salt links some 30 A away. The above, provides a structural basis for ligand binding synergism, effects on, k(cat) due to mutations far from the site of catalysis, and the complete, loss of substrate efficacy due to minor alterations of the 5'-phosphoryl, group of IMP.
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<StructureSection load='1kkf' size='340' side='right'caption='[[1kkf]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1kkf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KKF FirstGlance]. <br>
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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]] 2.6&#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=DPO:DIPHOSPHATE'>DPO</scene>, <scene name='pdbligand=HDA:HADACIDIN'>HDA</scene>, <scene name='pdbligand=IMP:INOSINIC+ACID'>IMP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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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=1kkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kkf OCA], [https://pdbe.org/1kkf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kkf RCSB], [https://www.ebi.ac.uk/pdbsum/1kkf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kkf ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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]
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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/kk/1kkf_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=1kkf ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1KKF 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, DPO, HAD and IMP 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KKF OCA].
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*[[Adenylosuccinate synthetase 3D structures|Adenylosuccinate synthetase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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IMP Alone Organizes the Active Site of Adenylosuccinate Synthetase from Escherichia coli., Hou Z, Wang W, Fromm HJ, Honzatko RB, J Biol Chem. 2002 Feb 22;277(8):5970-6. Epub 2001 Dec 12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11741996 11741996]
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[[Category: Escherichia coli K-12]]
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[[Category: Adenylosuccinate synthase]]
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[[Category: Large Structures]]
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[[Category: Escherichia coli]]
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[[Category: Fromm HJ]]
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[[Category: Single protein]]
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[[Category: Honzatko RB]]
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[[Category: Fromm, H.J.]]
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[[Category: Hou Z]]
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[[Category: Honzatko, R.B.]]
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[[Category: Wang W]]
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[[Category: Hou, Z.]]
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[[Category: Wang, W.]]
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[[Category: DPO]]
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[[Category: HAD]]
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[[Category: IMP]]
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[[Category: MG]]
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[[Category: gtp-hydrolysing enzymes]]
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[[Category: induced fit]]
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[[Category: ligase]]
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[[Category: purine nucleotide biosynthesis]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:19:33 2007''
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Current revision

Complex of E. coli Adenylosuccinate Synthetase with IMP, Hadacidin, Pyrophosphate, and Mg

PDB ID 1kkf

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