Sandbox Reserved 316

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 12: Line 12:
==Exploring the structure==
==Exploring the structure==
LovD is a 413-amino acid protein predicted to have an α/β hydrolase fold based on primary sequence analysis<ref name="paper2">PMID:10334994</ref>.
LovD is a 413-amino acid protein predicted to have an α/β hydrolase fold based on primary sequence analysis<ref name="paper2">PMID:10334994</ref>.
-
LovD has of two domains. The first domain, which consists of residues 1–92 and 204–413, is a central seven-stranded antiparallel β-sheet flanked by α-helices on either face<ref name="paper1">PMID:17277201</ref>. The second domain is smaller, consists of residues 93–203 and is primarily α-helical<ref name="paper1">PMID:17277201</ref>.
+
LovD has of two domains. The <scene name='Sandbox_Reserved_316/First_domain/1'>first domain</scene>, which consists of residues 1–92 and 204–413, is a central seven-stranded antiparallel β-sheet flanked by α-helices on either face<ref name="paper1">PMID:17277201</ref>. The second domain is smaller, consists of residues 93–203 and is primarily α-helical<ref name="paper1">PMID:17277201</ref>.
==References==
==References==
<references/>
<references/>
10334994
10334994

Revision as of 23:30, 23 March 2011

This Sandbox is Reserved from January 10, 2010, through April 10, 2011 for use in BCMB 307-Proteins course taught by Andrea Gorrell at the University of Northern British Columbia, Prince George, BC, Canada.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • Click the 3D button (when editing, above the wikitext box) to insert Jmol.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing


PDB ID 3hle

Drag the structure with the mouse to rotate
3hle, resolution 2.06Å ()
Ligands: ,
Related: 1hld
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml


Introduction

Simvastation synthase (LovD) is an enzyme isolated from the natural product biosynthetic pathways of Aspergillus terreus. Simvastatin Synthase is an acyltransferase that converts the inactive monacolin J acid () by dimethylbutyryl chloride to yield the protected form of simvastatin, which is subsequently undergoes lactonization to yield simvastatin. LovD can also synthesize the blockbuster drug simvastatin using MJA and a synthetic α-dimethylbutyryl thioester[1].

LovD can also synthesize the blockbuster drug simvastatin using MJA and a synthetic alpha-dimethylbutyryl thioester, albeit with suboptimal properties as a biocatalyst[1].

Exploring the structure

LovD is a 413-amino acid protein predicted to have an α/β hydrolase fold based on primary sequence analysis[2]. LovD has of two domains. The , which consists of residues 1–92 and 204–413, is a central seven-stranded antiparallel β-sheet flanked by α-helices on either face[1]. The second domain is smaller, consists of residues 93–203 and is primarily α-helical[1].

References

  1. ↑ 1.0 1.1 1.2 1.3 Xie X, Tang Y. Efficient synthesis of simvastatin by use of whole-cell biocatalysis. Appl Environ Microbiol. 2007 Apr;73(7):2054-60. Epub 2007 Feb 2. PMID:17277201 doi:10.1128/AEM.02820-06
  2. ↑ Kennedy J, Auclair K, Kendrew SG, Park C, Vederas JC, Hutchinson CR. Modulation of polyketide synthase activity by accessory proteins during lovastatin biosynthesis. Science. 1999 May 21;284(5418):1368-72. PMID:10334994

10334994

Retrieved from "http://52.214.119.220/wiki/index.php/Sandbox_Reserved_316"
Personal tools