1gxb
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The crystal structure of the dimeric anthranilate | + | The crystal structure of the dimeric anthranilate phosphoribosyltransferase (AnPRT) reveals a new category of phosphoribosyltransferases, designated as class III. The active site of this enzyme is located within the flexible hinge region of its two-domain structure. The pyrophosphate moiety of phosphoribosylpyrophosphate is co-ordinated by a metal ion and is bound by two conserved loop regions within this hinge region. With the structure of AnPRT available, structural analysis of all enzymatic activities of the tryptophan biosynthesis pathway is complete, thereby connecting the evolution of its enzyme members to the general development of metabolic processes. Its structure reveals it to have the same fold, topology, active site location and type of association as class II nucleoside phosphorylases. At the level of sequences, this relationship is mirrored by 13 structurally invariant residues common to both enzyme families. Taken together, these data imply common ancestry of enzymes catalysing reverse biological processes--the ribosylation and deribosylation of metabolic pathway intermediates. These relationships establish new links for enzymes involved in nucleotide and amino acid metabolism. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Kirschner, K.]] | [[Category: Kirschner, K.]] | ||
[[Category: Mayans, O.]] | [[Category: Mayans, O.]] | ||
| - | [[Category: Nissen, L | + | [[Category: Nissen, L J.]] |
[[Category: Wilmanns, M.]] | [[Category: Wilmanns, M.]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: tryptophane biosynthesis]] | [[Category: tryptophane biosynthesis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:55:00 2008'' |
Revision as of 10:55, 21 February 2008
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ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE IN COMPLEX WITH PYROPHOSPHATE AND MAGNESIUM
Overview
The crystal structure of the dimeric anthranilate phosphoribosyltransferase (AnPRT) reveals a new category of phosphoribosyltransferases, designated as class III. The active site of this enzyme is located within the flexible hinge region of its two-domain structure. The pyrophosphate moiety of phosphoribosylpyrophosphate is co-ordinated by a metal ion and is bound by two conserved loop regions within this hinge region. With the structure of AnPRT available, structural analysis of all enzymatic activities of the tryptophan biosynthesis pathway is complete, thereby connecting the evolution of its enzyme members to the general development of metabolic processes. Its structure reveals it to have the same fold, topology, active site location and type of association as class II nucleoside phosphorylases. At the level of sequences, this relationship is mirrored by 13 structurally invariant residues common to both enzyme families. Taken together, these data imply common ancestry of enzymes catalysing reverse biological processes--the ribosylation and deribosylation of metabolic pathway intermediates. These relationships establish new links for enzymes involved in nucleotide and amino acid metabolism.
About this Structure
1GXB is a Single protein structure of sequence from Sulfolobus solfataricus with and as ligands. Active as Transferase, with EC number 2.4.2.18. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structural analysis of two enzymes catalysing reverse metabolic reactions implies common ancestry., Mayans O, Ivens A, Nissen LJ, Kirschner K, Wilmanns M, EMBO J. 2002 Jul 1;21(13):3245-54. PMID:12093726
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