1dkr: Difference between revisions

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[[Image:1dkr.~~jpg~~|left|200px]]

[[Image:1dkr.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURES OF BACILLUS SUBTILIS PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE: MOLECULAR BASIS OF ALLOSTERIC INHIBITION AND ACTIVATION.~~'''~~

===CRYSTAL STRUCTURES OF BACILLUS SUBTILIS PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE: MOLECULAR BASIS OF ALLOSTERIC INHIBITION AND ACTIVATION.===

~~==Overview==~~

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Here we report the first three-dimensional structure of a phosphoribosylpyrophosphate (PRPP) synthetase. PRPP is an essential intermediate in several biosynthetic pathways. Structures of the Bacillus subtilis PRPP synthetase in complex with analogs of the activator phosphate and the allosteric inhibitor ADP show that the functional form of the enzyme is a hexamer. The ~~individual subunits fold into two domains~~, ~~both of which resemble~~ the ~~type I phosphoribosyltransfereases. The active site is located between~~ the ~~two domains and includes residues from two subunits~~. ~~Phosphate and ADP bind to the same regulatory site consisting of residues from three subunits of the hexamer~~. ~~In addition to identifying residues important for binding substrates and effectors~~, the ~~structures suggest a novel mode of allosteric regulation~~.

The line below this paragraph, {{ABSTRACT_PUBMED_10742175}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10742175 is the PubMed ID number.

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==About this Structure==

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[[Category: Open alpha beta domain structure]]

[[Category: Phosphoribosyltransferase type i fold.]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2~~ 13:~~57:47~~ 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:13:10 2008''

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-[[Image:1dkr.jpg|left|200px]]
+{{Seed}}
+[[Image:1dkr.png|left|200px]]
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 {{STRUCTURE_1dkr|  PDB=1dkr  |  SCENE=  }}
-'''CRYSTAL STRUCTURES OF BACILLUS SUBTILIS PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE: MOLECULAR BASIS OF ALLOSTERIC INHIBITION AND ACTIVATION.'''
+===CRYSTAL STRUCTURES OF BACILLUS SUBTILIS PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE: MOLECULAR BASIS OF ALLOSTERIC INHIBITION AND ACTIVATION.===
-==Overview==
+<!--
-Here we report the first three-dimensional structure of a phosphoribosylpyrophosphate (PRPP) synthetase. PRPP is an essential intermediate in several biosynthetic pathways. Structures of the Bacillus subtilis PRPP synthetase in complex with analogs of the activator phosphate and the allosteric inhibitor ADP show that the functional form of the enzyme is a hexamer. The individual subunits fold into two domains, both of which resemble the type I phosphoribosyltransfereases. The active site is located between the two domains and includes residues from two subunits. Phosphate and ADP bind to the same regulatory site consisting of residues from three subunits of the hexamer. In addition to identifying residues important for binding substrates and effectors, the structures suggest a novel mode of allosteric regulation.
+The line below this paragraph, {{ABSTRACT_PUBMED_10742175}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10742175 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10742175}}
 ==About this Structure==
@@ Line 31: / Line 35: @@
 [[Category: Open alpha beta domain structure]]
 [[Category: Phosphoribosyltransferase type i fold.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:57:47 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:13:10 2008''