1i9a
From Proteopedia
(New page: 200px<br /><applet load="1i9a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i9a, resolution 2.5Å" /> '''STRUCTURAL STUDIES OF...) |
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| - | [[Image:1i9a.gif|left|200px]]<br /><applet load="1i9a" size=" | + | [[Image:1i9a.gif|left|200px]]<br /><applet load="1i9a" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1i9a, resolution 2.5Å" /> | caption="1i9a, resolution 2.5Å" /> | ||
'''STRUCTURAL STUDIES OF CHOLESTEROL BIOSYNTHESIS: MEVALONATE 5-DIPHOSPHATE DECARBOXYLASE AND ISOPENTENYL DIPHOSPHATE ISOMERASE'''<br /> | '''STRUCTURAL STUDIES OF CHOLESTEROL BIOSYNTHESIS: MEVALONATE 5-DIPHOSPHATE DECARBOXYLASE AND ISOPENTENYL DIPHOSPHATE ISOMERASE'''<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== | ||
| - | 1I9A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Isopentenyl-diphosphate_Delta-isomerase Isopentenyl-diphosphate Delta-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.3.2 5.3.3.2] Full crystallographic information is available from [http:// | + | 1I9A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Isopentenyl-diphosphate_Delta-isomerase Isopentenyl-diphosphate Delta-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.3.2 5.3.3.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I9A OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Isopentenyl-diphosphate Delta-isomerase]] | [[Category: Isopentenyl-diphosphate Delta-isomerase]] | ||
[[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: MN]] | [[Category: MN]] | ||
[[Category: alpha/beta protein]] | [[Category: alpha/beta protein]] | ||
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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 13:09:21 2008'' |
Revision as of 11:09, 21 February 2008
|
STRUCTURAL STUDIES OF CHOLESTEROL BIOSYNTHESIS: MEVALONATE 5-DIPHOSPHATE DECARBOXYLASE AND ISOPENTENYL DIPHOSPHATE ISOMERASE
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
1I9A is a Single protein structure of sequence from Escherichia coli with as ligand. Active as Isopentenyl-diphosphate Delta-isomerase, with EC number 5.3.3.2 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 13:09:21 2008
Categories: Escherichia coli | Isopentenyl-diphosphate Delta-isomerase | 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. | MN | Alpha/beta protein | Isomerase | Mn2+ | New york structural genomix research consortium | Nysgxrc | Protein structure initiative | Psi | Structural genomics
