1vg4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1vg4.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1vg4.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1vg4| PDB=1vg4 | SCENE= }}
{{STRUCTURE_1vg4| PDB=1vg4 | SCENE= }}
-
'''Crystal Structure Of Octaprenyl Pyrophosphate Synthase From Hyperthermophilic Thermotoga Maritima F132A/L128A mutant'''
+
===Crystal Structure Of Octaprenyl Pyrophosphate Synthase From Hyperthermophilic Thermotoga Maritima F132A/L128A mutant===
-
==Overview==
+
<!--
-
Octaprenyl pyrophosphate synthase (OPPs) catalyzes consecutive condensation reactions of farnesyl pyrophosphate (FPP) with five molecules of isopentenyl pyrophosphate (IPP) to generate C(40) octaprenyl pyrophosphate (OPP) which constitutes the side chain of menaquinone. We have previously reported the X-ray structure of OPPs from Thermotoga maritima, which is composed entirely of alpha-helices joined by connecting loops and is arranged with nine core helices around a large central cavity [Guo, R. T., Kuo, C. J., Ko, T. P., Chou, C. C., Shr, R. L., Liang, P. H., and Wang, A. H.-J. (2004) J. Biol. Chem. 279, 4903-4912]. A76 and S77 are located on top of the active site close to where FPP is bound. A76Y and A76Y/S77F OPPs mutants produce C(20), indicating that the substituted larger residues interfere with the substrate chain elongation. Surprisingly, the A76Y/S77F mutant synthesizes a larger amount of C(20) than the A76Y mutant. In the crystal structure of the A76Y/S77F mutant, F77 is pushed away by Y76, thereby creating more space between those two large amino acids to accommodate the C(20) product. A large F132 residue at the bottom of the tunnel-shaped active site serves as the "floor" and determines the final product chain length. The substitution of F132 with a small Ala, thereby removing the blockade, led to the synthesis of a C(50) product larger than that produced by the wild-type enzyme. On the basis of the structure, we have sequentially mutated the large amino acids, including F132, L128, I123, and D62, to Ala underneath the tunnel. The products of the F132A/L128A/I123A/D62A mutant reach C(95), beyond the largest chain length generated by all known trans-prenyltransferases. Further modifications of the enzyme reaction conditions, including new IPP derivatives, may allow the preparation of high-molecular weight polyprenyl products resembling the rubber molecule.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15196010}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15196010 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15196010}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Thermophilic]]
[[Category: Thermophilic]]
[[Category: Trans-type prenyltransferase]]
[[Category: Trans-type prenyltransferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:30:08 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:24:55 2008''

Revision as of 04:25, 29 July 2008

Image:1vg4.png

Template:STRUCTURE 1vg4

Crystal Structure Of Octaprenyl Pyrophosphate Synthase From Hyperthermophilic Thermotoga Maritima F132A/L128A mutant

Template:ABSTRACT PUBMED 15196010

About this Structure

1VG4 is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

Reference

A molecular ruler for chain elongation catalyzed by octaprenyl pyrophosphate synthase and its structure-based engineering to produce unprecedented long chain trans-prenyl products., Guo RT, Kuo CJ, Ko TP, Chou CC, Liang PH, Wang AH, Biochemistry. 2004 Jun 22;43(24):7678-86. PMID:15196010

Page seeded by OCA on Tue Jul 29 07:24:55 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1vg4"
Personal tools