1hoo
From Proteopedia
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| - | [[Image:1hoo.gif|left|200px]] | + | [[Image:1hoo.gif|left|200px]] |
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| - | '''STRUCTURE OF GUANINE NUCLEOTIDE (GPPCP) COMPLEX OF ADENYLOSUCCINATE SYNTHETASE FROM E. COLI AT PH 6.5 AND 25 DEGREES CELSIUS''' | + | {{Structure |
| + | |PDB= 1hoo |SIZE=350|CAPTION= <scene name='initialview01'>1hoo</scene>, resolution 2.3Å | ||
| + | |SITE= <scene name='pdbsite=GNA:These+Residues+Make+Up+The+Guanine+Nucleotide+Binding+Si+...'>GNA</scene> and <scene name='pdbsite=GNB:These+Residues+Make+Up+The+Guanine+Nucleotide+Binding+Si+...'>GNB</scene> | ||
| + | |LIGAND= <scene name='pdbligand=GNH:AMINOPHOSPHONIC ACID-GUANYLATE ESTER'>GNH</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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE OF GUANINE NUCLEOTIDE (GPPCP) COMPLEX OF ADENYLOSUCCINATE SYNTHETASE FROM E. COLI AT PH 6.5 AND 25 DEGREES CELSIUS''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HOO is a [ | + | 1HOO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HOO OCA]. |
==Reference== | ==Reference== | ||
| - | Refined crystal structures of guanine nucleotide complexes of adenylosuccinate synthetase from Escherichia coli., Poland BW, Hou Z, Bruns C, Fromm HJ, Honzatko RB, J Biol Chem. 1996 Jun 28;271(26):15407-13. PMID:[http:// | + | Refined crystal structures of guanine nucleotide complexes of adenylosuccinate synthetase from Escherichia coli., Poland BW, Hou Z, Bruns C, Fromm HJ, Honzatko RB, J Biol Chem. 1996 Jun 28;271(26):15407-13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8663109 8663109] |
[[Category: Adenylosuccinate synthase]] | [[Category: Adenylosuccinate synthase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: Poland, B W.]] | [[Category: Poland, B W.]] | ||
[[Category: GNH]] | [[Category: GNH]] | ||
| - | [[Category: gtp-hydrolysing | + | [[Category: gtp-hydrolysing enzyme]] |
[[Category: ligase]] | [[Category: ligase]] | ||
[[Category: purine nucleotide biosynthesis]] | [[Category: purine nucleotide biosynthesis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:39:41 2008'' |
Revision as of 09:39, 20 March 2008
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| , resolution 2.3Å | |||||||
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| Sites: | and | ||||||
| Ligands: | |||||||
| Activity: | Adenylosuccinate synthase, with EC number 6.3.4.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF GUANINE NUCLEOTIDE (GPPCP) COMPLEX OF ADENYLOSUCCINATE SYNTHETASE FROM E. COLI AT PH 6.5 AND 25 DEGREES CELSIUS
Overview
Structures of adenylosuccinate synthetase from Escherichia coli complexed with guanosine-5'-(beta,gamma-imido) triphosphate and guanosine-5'-(beta,gamma-methylene)triphosphate in the presence and the absence of Mg2+ have been refined to R-factors below 0.2 against data to a nominal resolution of 2.7 A. Asp333 of the synthetase hydrogen bonds to the exocyclic 2-amino and endocyclic N1 groups of the guanine nucleotide base, whereas the hydroxyl of Ser414 and the backbone amide of Lys331 hydrogen bond to the 6-oxo position. The side chains of Lys331 and Pro417 pack against opposite faces of the guanine nucleotide base. The synthetase recognizes neither the N7 position of guanine nucleotides nor the ribose group. Electron density for the guanine-5'-(beta,gamma-imido) triphosphate complex is consistent with a mixture of the triphosphate nucleoside and its hydrolyzed diphosphate nucleoside bound to the active site. The base, ribose, and alpha-phosphate positions overlap, but the beta-phosphates occupy different binding sites. The binding of guanosine-5'-(beta,gamma-methylene)triphosphate to the active site is comparable with that of guanosine-5'-(beta, gamma-imido)triphosphate. No electron density, however, for the corresponding diphosphate nucleoside is observed. In addition, electron density for bound Mg2+ is absent in these nucleotide complexes. The guanine nucleotide complexes of the synthetase are compared with complexes of other GTP-binding proteins and to a preliminary structure of the complex of GDP, IMP, Mg2+, and succinate with the synthetase. The enzyme, under conditions reported here, does not undergo a conformational change in response to the binding of guanine nucleotides, and minimally IMP and/or Mg2+ must be present in order to facilitate the complete recognition of the guanine nucleotide by the synthetase.
About this Structure
1HOO is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Refined crystal structures of guanine nucleotide complexes of adenylosuccinate synthetase from Escherichia coli., Poland BW, Hou Z, Bruns C, Fromm HJ, Honzatko RB, J Biol Chem. 1996 Jun 28;271(26):15407-13. PMID:8663109
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