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1gin
From Proteopedia
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| - | [[Image:1gin. | + | [[Image:1gin.jpg|left|200px]]<br /><applet load="1gin" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1gin" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1gin, resolution 2.8Å" /> | caption="1gin, resolution 2.8Å" /> | ||
'''CRYSTAL STRUCTURE OF ADENYLOSUCCINATE SYNTHETASE FROM ESCHERICHIA COLI COMPLEXED WITH GDP, IMP, HADACIDIN, NO3-, AND MG2+. DATA COLLECTED AT 298K (PH 6.5).'''<br /> | '''CRYSTAL STRUCTURE OF ADENYLOSUCCINATE SYNTHETASE FROM ESCHERICHIA COLI COMPLEXED WITH GDP, IMP, HADACIDIN, NO3-, AND MG2+. DATA COLLECTED AT 298K (PH 6.5).'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 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] | + | 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] Known structural/functional Sites: <scene name='pdbsite=ASP:These Residues Make Up The Guanine Nucleotide Binding Si ...'>ASP</scene>, <scene name='pdbsite=GNS:These Residues Make Up The Guanine Nucleotide Binding Si ...'>GNS</scene> and <scene name='pdbsite=IMP:These Residues Make Up The Guanine Nucleotide Binding Si ...'>IMP</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GIN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: purine nucleotide biosynthesis]] | [[Category: purine nucleotide biosynthesis]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 15:19:34 2007'' |
Revision as of 13:09, 18 December 2007
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CRYSTAL STRUCTURE OF ADENYLOSUCCINATE SYNTHETASE FROM ESCHERICHIA COLI COMPLEXED WITH GDP, IMP, HADACIDIN, NO3-, AND MG2+. DATA COLLECTED AT 298K (PH 6.5).
Overview
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 GDP, NO3-, and Mg2+ suggest an interaction between the beta,gamma-bridging oxygen, atom of GTP and Mg2+ in the enzyme-substrate complex. His41 hydrogen bonds, to the beta-phosphate group of GDP and approaches bound NO3-. The aldehyde, group of hadacidin coordinates to the Mg2+, while its carboxyl group, interacts with backbone amide groups 299 to 303 and the side-chain of, Arg303. The 5'-phosphate group of IMP interacts with Asn38, Thr129, Thr239, and Arg143 (from a monomer related by 2-fold symmetry). A mechanism is, proposed for the two-step reaction governed by the synthetase, in which, His41 and Asp13 are essential catalytic side-chains.
About this Structure
1GIN is a Single protein structure of sequence from Escherichia coli with MG, NO3, HAD, IMP and GDP as ligands. Active as Adenylosuccinate synthase, with EC number 6.3.4.4 Known structural/functional Sites: , and . Full crystallographic information is available from OCA.
Reference
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:9000627
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