1gph

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[[Image:1gph.gif|left|200px]]
[[Image:1gph.gif|left|200px]]
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{{Structure
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|PDB= 1gph |SIZE=350|CAPTION= <scene name='initialview01'>1gph</scene>, resolution 3.0&Aring;
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The line below this paragraph, containing "STRUCTURE_1gph", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Amidophosphoribosyltransferase Amidophosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.14 2.4.2.14] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1gph| PDB=1gph | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gph OCA], [http://www.ebi.ac.uk/pdbsum/1gph PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gph RCSB]</span>
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}}
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'''STRUCTURE OF THE ALLOSTERIC REGULATORY ENZYME OF PURINE BIOSYNTHESIS'''
'''STRUCTURE OF THE ALLOSTERIC REGULATORY ENZYME OF PURINE BIOSYNTHESIS'''
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Smith, J L.]]
[[Category: Smith, J L.]]
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[[Category: transferase(glutamine amidotransferase)]]
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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 Sun Mar 30 20:48:56 2008''
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Revision as of 14:51, 2 May 2008

Image:1gph.gif

Template:STRUCTURE 1gph

STRUCTURE OF THE ALLOSTERIC REGULATORY ENZYME OF PURINE BIOSYNTHESIS


Overview

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.

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 Fri May 2 17:51:24 2008

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