1fi4
From Proteopedia
(New page: 200px<br /><applet load="1fi4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fi4, resolution 2.27Å" /> '''THE X-RAY CRYSTAL ST...) |
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| - | [[Image:1fi4.gif|left|200px]]<br /><applet load="1fi4" size=" | + | [[Image:1fi4.gif|left|200px]]<br /><applet load="1fi4" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fi4, resolution 2.27Å" /> | caption="1fi4, resolution 2.27Å" /> | ||
'''THE X-RAY CRYSTAL STRUCTURE OF MEVALONATE 5-DIPHOSPHATE DECARBOXYLASE AT 2.3 ANGSTROM RESOLUTION.'''<br /> | '''THE X-RAY CRYSTAL STRUCTURE OF MEVALONATE 5-DIPHOSPHATE DECARBOXYLASE AT 2.3 ANGSTROM RESOLUTION.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | X-ray structures of two enzymes in the sterol/isoprenoid biosynthesis | + | X-ray structures of two enzymes in the sterol/isoprenoid biosynthesis pathway have been determined in a structural genomics pilot study. Mevalonate-5-diphosphate decarboxylase (MDD) is a single-domain alpha/beta protein that catalyzes the last of three sequential ATP-dependent reactions which convert mevalonate to isopentenyl diphosphate. Isopentenyl disphosphate isomerase (IDI) is an alpha/beta metalloenzyme that catalyzes interconversion of isopentenyl diphosphate and dimethylallyl diphosphate, which condense in the next step toward synthesis of sterols and a host of natural products. Homology modeling of related proteins and comparisons of the MDD and IDI structures with two other experimentally determined structures have shown that MDD is a member of the GHMP superfamily of small-molecule kinases and IDI is similar to the nudix hydrolases, which act on nucleotide diphosphatecontaining substrates. Structural models were produced for 379 proteins, encompassing a substantial fraction of both protein superfamilies. All three enzymes responsible for synthesis of isopentenyl diphosphate from mevalonate (mevalonate kinase, phosphomevalonate kinase, and MDD) share the same fold, catalyze phosphorylation of chemically similar substrates (MDD decarboxylation involves phosphorylation of mevalonate diphosphate), and seem to have evolved from a common ancestor. These structures and the structural models derived from them provide a framework for interpreting biochemical function and evolutionary relationships. |
==About this Structure== | ==About this Structure== | ||
| - | 1FI4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Active as [http://en.wikipedia.org/wiki/Diphosphomevalonate_decarboxylase Diphosphomevalonate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.33 4.1.1.33] Full crystallographic information is available from [http:// | + | 1FI4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Active as [http://en.wikipedia.org/wiki/Diphosphomevalonate_decarboxylase Diphosphomevalonate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.33 4.1.1.33] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FI4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bonanno, J | + | [[Category: Bonanno, J B.]] |
| - | [[Category: Burley, S | + | [[Category: Burley, S K.]] |
[[Category: Edo, C.]] | [[Category: Edo, C.]] | ||
[[Category: Eswar, N.]] | [[Category: Eswar, N.]] | ||
| - | [[Category: Gerchman, S | + | [[Category: Gerchman, S E.]] |
[[Category: Ilyin, V.]] | [[Category: Ilyin, V.]] | ||
[[Category: Kycia, H.]] | [[Category: Kycia, H.]] | ||
| - | [[Category: NYSGXRC, New | + | [[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]] |
[[Category: Pieper, U.]] | [[Category: Pieper, U.]] | ||
| - | [[Category: Romanowski, M | + | [[Category: Romanowski, M J.]] |
[[Category: Sali, A.]] | [[Category: Sali, A.]] | ||
| - | [[Category: Studier, F | + | [[Category: Studier, F W.]] |
[[Category: atp binding]] | [[Category: atp binding]] | ||
[[Category: cholesterol biosynthesis]] | [[Category: cholesterol biosynthesis]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:39:01 2008'' |
Revision as of 10:39, 21 February 2008
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THE X-RAY CRYSTAL STRUCTURE OF MEVALONATE 5-DIPHOSPHATE DECARBOXYLASE AT 2.3 ANGSTROM RESOLUTION.
Overview
X-ray structures of two enzymes in the sterol/isoprenoid biosynthesis pathway have been determined in a structural genomics pilot study. Mevalonate-5-diphosphate decarboxylase (MDD) is a single-domain alpha/beta protein that catalyzes the last of three sequential ATP-dependent reactions which convert mevalonate to isopentenyl diphosphate. Isopentenyl disphosphate isomerase (IDI) is an alpha/beta metalloenzyme that catalyzes interconversion of isopentenyl diphosphate and dimethylallyl diphosphate, which condense in the next step toward synthesis of sterols and a host of natural products. Homology modeling of related proteins and comparisons of the MDD and IDI structures with two other experimentally determined structures have shown that MDD is a member of the GHMP superfamily of small-molecule kinases and IDI is similar to the nudix hydrolases, which act on nucleotide diphosphatecontaining substrates. Structural models were produced for 379 proteins, encompassing a substantial fraction of both protein superfamilies. All three enzymes responsible for synthesis of isopentenyl diphosphate from mevalonate (mevalonate kinase, phosphomevalonate kinase, and MDD) share the same fold, catalyze phosphorylation of chemically similar substrates (MDD decarboxylation involves phosphorylation of mevalonate diphosphate), and seem to have evolved from a common ancestor. These structures and the structural models derived from them provide a framework for interpreting biochemical function and evolutionary relationships.
About this Structure
1FI4 is a Single protein structure of sequence from Saccharomyces cerevisiae. Active as Diphosphomevalonate decarboxylase, with EC number 4.1.1.33 Full crystallographic information is available from OCA.
Reference
Structural genomics of enzymes involved in sterol/isoprenoid biosynthesis., Bonanno JB, Edo C, Eswar N, Pieper U, Romanowski MJ, Ilyin V, Gerchman SE, Kycia H, Studier FW, Sali A, Burley SK, Proc Natl Acad Sci U S A. 2001 Nov 6;98(23):12896-901. PMID:11698677
Page seeded by OCA on Thu Feb 21 12:39:01 2008
Categories: Diphosphomevalonate decarboxylase | Saccharomyces cerevisiae | Single protein | Bonanno, J B. | Burley, S K. | Edo, C. | Eswar, N. | Gerchman, S E. | Ilyin, V. | Kycia, H. | NYSGXRC, New York Structural GenomiX Research Consortium. | Pieper, U. | Romanowski, M J. | Sali, A. | Studier, F W. | Atp binding | Cholesterol biosynthesis | Decarboxylase | Mixed alpha/beta structure | New york structural genomix research consortium | Nysgxrc | Protein structure initiative | Psi | Structural genomics
