1kkf: Difference between revisions

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<StructureSection load='1kkf' size='340' side='right'caption='[[1kkf]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='1kkf' size='340' side='right'caption='[[1kkf]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1kkf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. 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>
<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>
</td></tr><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>
</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>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1cib|1cib]], [[1kjx|1kjx]], [[1kkb|1kkb]]</div></td></tr>
<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>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Adenylosuccinate_synthase Adenylosuccinate synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.4 6.3.4.4] </span></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=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>
<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>
</table>
</table>
== Function ==
== 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]  
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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].
</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].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:11741996<ref>PMID:11741996</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1kkf" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Adenylosuccinate synthetase 3D structures|Adenylosuccinate synthetase 3D structures]]
*[[Adenylosuccinate synthetase 3D structures|Adenylosuccinate synthetase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Adenylosuccinate synthase]]
[[Category: Escherichia coli K-12]]
[[Category: Ecoli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Fromm, H J]]
[[Category: Fromm HJ]]
[[Category: Honzatko, R B]]
[[Category: Honzatko RB]]
[[Category: Hou, Z]]
[[Category: Hou Z]]
[[Category: Wang, W]]
[[Category: Wang W]]
[[Category: Gtp-hydrolysing enzyme]]
[[Category: Induced fit]]
[[Category: Ligase]]
[[Category: Purine nucleotide biosynthesis]]

Latest revision as of 10:25, 14 February 2024

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

Structural highlights

1kkf is a 1 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1kkf, resolution 2.60Å

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