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1gph

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{{STRUCTURE_1gph| PDB=1gph | SCENE= }}
{{STRUCTURE_1gph| PDB=1gph | SCENE= }}
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'''STRUCTURE OF THE ALLOSTERIC REGULATORY ENZYME OF PURINE BIOSYNTHESIS'''
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===STRUCTURE OF THE ALLOSTERIC REGULATORY ENZYME OF PURINE BIOSYNTHESIS===
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==Overview==
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Multi-wavelength anomalous diffraction (MAD) has been used to determine the structure of the regulatory enzyme of de novo synthesis of purine nucleotides, glutamine 5-phosphoribosyl-1-pyrophosphate (PRPP) amidotransferase, from Bacillus subtilis. This allosteric enzyme, a 200-kilodalton tetramer, is subject to end product regulation by purine nucleotides. The metalloenzyme from B. subtilis is a paradigm for the higher eukaryotic enzymes, which have been refractory to isolation in stable form. The two folding domains of the polypeptide are correlated with functional domains for glutamine binding and for transfer of ammonia to the substrate PRPP. Eight molecules of the feedback inhibitor adenosine monophosphate (AMP) are bound to the tetrameric enzyme in two types of binding sites: the PRPP catalytic site of each subunit and an unusual regulatory site that is immediately adjacent to each active site but is between subunits. An oxygen-sensitive [4Fe-4S] cluster in each subunit is proposed to regulate protein turnover in vivo and is distant from the catalytic site. Oxygen sensitivity of the cluster is diminished by AMP, which blocks a channel through the protein to the cluster. The structure is representative of both glutamine amidotransferases and phosphoribosyltransferases.
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(as it appears on PubMed at http://www.pubmed.gov), where 8197456 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8197456}}
==About this Structure==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Smith, J L.]]
[[Category: Smith, J L.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:51:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:38:50 2008''

Revision as of 02:38, 1 July 2008

Image:1gph.png

Template:STRUCTURE 1gph

STRUCTURE OF THE ALLOSTERIC REGULATORY ENZYME OF PURINE BIOSYNTHESIS

Template:ABSTRACT PUBMED 8197456

About this Structure

1GPH is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

Structure of the allosteric regulatory enzyme of purine biosynthesis., Smith JL, Zaluzec EJ, Wery JP, Niu L, Switzer RL, Zalkin H, Satow Y, Science. 1994 Jun 3;264(5164):1427-33. PMID:8197456

Page seeded by OCA on Tue Jul 1 05:38:50 2008

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