1fi4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1fi4.gif|left|200px]]<br /><applet load="1fi4" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1fi4.gif|left|200px]]
-
caption="1fi4, resolution 2.27&Aring;" />
+
 
-
'''THE X-RAY CRYSTAL STRUCTURE OF MEVALONATE 5-DIPHOSPHATE DECARBOXYLASE AT 2.3 ANGSTROM RESOLUTION.'''<br />
+
{{Structure
 +
|PDB= 1fi4 |SIZE=350|CAPTION= <scene name='initialview01'>1fi4</scene>, resolution 2.27&Aring;
 +
|SITE=
 +
|LIGAND=
 +
|ACTIVITY= [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]
 +
|GENE=
 +
}}
 +
 
 +
'''THE X-RAY CRYSTAL STRUCTURE OF MEVALONATE 5-DIPHOSPHATE DECARBOXYLASE AT 2.3 ANGSTROM RESOLUTION.'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==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://oca.weizmann.ac.il/oca-bin/ocashort?id=1FI4 OCA].
+
1FI4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FI4 OCA].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11698677 11698677]
+
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:[http://www.ncbi.nlm.nih.gov/pubmed/11698677 11698677]
[[Category: Diphosphomevalonate decarboxylase]]
[[Category: Diphosphomevalonate decarboxylase]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
Line 34: Line 43:
[[Category: protein structure initiative]]
[[Category: protein structure initiative]]
[[Category: psi]]
[[Category: psi]]
-
[[Category: structural genomics]]
+
[[Category: structural genomic]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:39:01 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:09:23 2008''

Revision as of 09:09, 20 March 2008

Image:1fi4.gif


PDB ID 1fi4

Drag the structure with the mouse to rotate
, resolution 2.27Å
Activity: Diphosphomevalonate decarboxylase, with EC number 4.1.1.33
Coordinates: save as pdb, mmCIF, xml



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. 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 Mar 20 11:09:23 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1fi4"
Personal tools