1dkr
From Proteopedia
(New page: 200px<br /><applet load="1dkr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dkr, resolution 2.30Å" /> '''CRYSTAL STRUCTURES O...) |
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| - | [[Image:1dkr.jpg|left|200px]]<br /><applet load="1dkr" size=" | + | [[Image:1dkr.jpg|left|200px]]<br /><applet load="1dkr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dkr, resolution 2.30Å" /> | caption="1dkr, resolution 2.30Å" /> | ||
'''CRYSTAL STRUCTURES OF BACILLUS SUBTILIS PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE: MOLECULAR BASIS OF ALLOSTERIC INHIBITION AND ACTIVATION.'''<br /> | '''CRYSTAL STRUCTURES OF BACILLUS SUBTILIS PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE: MOLECULAR BASIS OF ALLOSTERIC INHIBITION AND ACTIVATION.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Here we report the first three-dimensional structure of a | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1DKR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Ribose-phosphate_diphosphokinase Ribose-phosphate diphosphokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.6.1 2.7.6.1] Full crystallographic information is available from [http:// | + | 1DKR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Ribose-phosphate_diphosphokinase Ribose-phosphate diphosphokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.6.1 2.7.6.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DKR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Ribose-phosphate diphosphokinase]] | [[Category: Ribose-phosphate diphosphokinase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bentsen, A | + | [[Category: Bentsen, A K.]] |
| - | [[Category: Eriksen, T | + | [[Category: Eriksen, T A.]] |
| - | [[Category: Harlow, K | + | [[Category: Harlow, K W.]] |
[[Category: Kadziola, A.]] | [[Category: Kadziola, A.]] | ||
[[Category: Larsen, S.]] | [[Category: Larsen, S.]] | ||
| Line 24: | Line 24: | ||
[[Category: phosphoribosyltransferase type i fold.]] | [[Category: phosphoribosyltransferase type i fold.]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:17:49 2008'' |
Revision as of 10:17, 21 February 2008
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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.
About this Structure
1DKR is a Single protein structure of sequence from Bacillus subtilis with as ligand. Active as Ribose-phosphate diphosphokinase, with EC number 2.7.6.1 Full crystallographic information is available from OCA.
Reference
Structural basis for the function of Bacillus subtilis phosphoribosyl-pyrophosphate synthetase., Eriksen TA, Kadziola A, Bentsen AK, Harlow KW, Larsen S, Nat Struct Biol. 2000 Apr;7(4):303-8. PMID:10742175
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