1cg3: Difference between revisions

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|PDB= 1cg3 |SIZE=350|CAPTION= <scene name='initialview01'>1cg3</scene>, resolution 2.5&Aring;
|PDB= 1cg3 |SIZE=350|CAPTION= <scene name='initialview01'>1cg3</scene>, resolution 2.5&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=HDA:HADACIDIN'>HDA</scene>, <scene name='pdbligand=IMO:6-O-PHOSPHORYL+INOSINE+MONOPHOSPHATE'>IMO</scene> and <scene name='pdbligand=GDP:GUANOSINE-5&#39;-DIPHOSPHATE'>GDP</scene>
|LIGAND= <scene name='pdbligand=GDP:GUANOSINE-5&#39;-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=HDA:HADACIDIN'>HDA</scene>, <scene name='pdbligand=IMO:6-O-PHOSPHORYL+INOSINE+MONOPHOSPHATE'>IMO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
|ACTIVITY= [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]  
|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cg3 OCA], [http://www.ebi.ac.uk/pdbsum/1cg3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cg3 RCSB]</span>
}}
}}


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[[Category: Honzatko, R.]]
[[Category: Honzatko, R.]]
[[Category: Poland, B W.]]
[[Category: Poland, B W.]]
[[Category: GDP]]
[[Category: HDA]]
[[Category: IMO]]
[[Category: MG]]
[[Category: 6-phosporyl- imp]]
[[Category: 6-phosporyl- imp]]
[[Category: gtp-hydrolysing enzyme]]
[[Category: gtp-hydrolysing enzyme]]
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[[Category: purine 2 nucleotide biosynthesis]]
[[Category: purine 2 nucleotide biosynthesis]]


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Revision as of 19:21, 30 March 2008

File:1cg3.jpg


PDB ID 1cg3

Drag the structure with the mouse to rotate
, resolution 2.5Å
Ligands: , , ,
Activity: Adenylosuccinate synthase, with EC number 6.3.4.4
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF THE MUTANT (R143L) OF ADENYLOSUCCINATE SYNTHETASE FROM E. COLI COMPLEXED WITH HADACIDIN, GDP, 6-PHOSPHORYL-IMP, AND MG2+


OverviewOverview

Asp13 and His41 are essential residues of adenylosuccinate synthetase, putatively catalyzing the formation of adenylosuccinate from an intermediate of 6-phosphoryl-IMP. Wild-type adenylosuccinate synthetase and three mutant synthetases (Arg143 --> Leu, Lys16 --> Gln, and Arg303 --> Leu) from Eschericha coli have been crystallized in the presence of IMP, hadacidin (an analogue of L-aspartate), Mg2+, and GTP. The active site of each complex contains 6-phosphoryl-IMP, Mg2+, GDP, and hadacidin, except for the Arg303 --> Leu mutant, which does not bind hadacidin. In response to the formation of 6-phosphoryl-IMP, Asp13 enters the inner coordination sphere of the active site Mg2+. His41 hydrogen bonds with 6-phosphoryl-IMP, except in the Arg303 --> Leu complex, where it remains bound to the guanine nucleotide. Hence, recognition of the active site Mg2+ by Asp13 evidently occurs after the formation of 6-phosphoryl-IMP, but recognition of the intermediate by His41 may require the association of L-aspartate with the active site. Structures reported here support a mechanism in which Asp13 and His41 act as the catalytic base and acid, respectively, in the formation of 6-phosphoryl-IMP, and then act together as catalytic acids in the subsequent formation of adenylosuccinate.

About this StructureAbout this Structure

1CG3 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Mechanistic implications from crystalline complexes of wild-type and mutant adenylosuccinate synthetases from Escherichia coli., Choe JY, Poland BW, Fromm HJ, Honzatko RB, Biochemistry. 1999 May 25;38(21):6953-61. PMID:10346917

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