Structure of Thermus thermophilus type 2 isopentenyl diphosphate isomerase inferred from crystallography and molecular dynamics

J. De Ruyck; S.C. Rothman; C.D. Poulter; J. Wouters

doi:10.1016/j.bbrc.2005.10.114

Structure of Thermus thermophilus type 2 isopentenyl diphosphate isomerase inferred from crystallography and molecular dynamics

J. De Ruyck, S.C. Rothman, C.D. Poulter, J. Wouters

Namur Research Institute for Life Sciences

Research output: Contribution to journal › Article › peer-review

Abstract

Crystal structures of Thermus thermophilus and Bacillus subtilis type 2 IPP isomerases were combined to generate an almost complete model of the FMN-bound structure of the enzyme. In contrast to previous studies, positions of flexible loops were obtained and carefully analyzed by molecular dynamics. Docking simulations find a unique putative binding site for the IPP substrate.

Original language	English
Pages (from-to)	1515-1518
Number of pages	4
Journal	Biochemical and Biophysical Research Communications
Volume	338
Issue number	3
DOIs	https://doi.org/10.1016/j.bbrc.2005.10.114
Publication status	Published - 23 Dec 2005

Access to Document

10.1016/j.bbrc.2005.10.114

Cite this

@article{d7b2f2f3acd748ae8070824d5922752c,

title = "Structure of Thermus thermophilus type 2 isopentenyl diphosphate isomerase inferred from crystallography and molecular dynamics",

abstract = "Crystal structures of Thermus thermophilus and Bacillus subtilis type 2 IPP isomerases were combined to generate an almost complete model of the FMN-bound structure of the enzyme. In contrast to previous studies, positions of flexible loops were obtained and carefully analyzed by molecular dynamics. Docking simulations find a unique putative binding site for the IPP substrate.",

author = "{De Ruyck}, J. and S.C. Rothman and C.D. Poulter and J. Wouters",

note = "MEDLINE{\textregistered} is the source for the MeSH terms of this document.",

year = "2005",

month = dec,

day = "23",

doi = "10.1016/j.bbrc.2005.10.114",

language = "English",

volume = "338",

pages = "1515--1518",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "3",

}

TY - JOUR

T1 - Structure of Thermus thermophilus type 2 isopentenyl diphosphate isomerase inferred from crystallography and molecular dynamics

AU - De Ruyck, J.

AU - Rothman, S.C.

AU - Poulter, C.D.

AU - Wouters, J.

N1 - MEDLINE® is the source for the MeSH terms of this document.

PY - 2005/12/23

Y1 - 2005/12/23

N2 - Crystal structures of Thermus thermophilus and Bacillus subtilis type 2 IPP isomerases were combined to generate an almost complete model of the FMN-bound structure of the enzyme. In contrast to previous studies, positions of flexible loops were obtained and carefully analyzed by molecular dynamics. Docking simulations find a unique putative binding site for the IPP substrate.

AB - Crystal structures of Thermus thermophilus and Bacillus subtilis type 2 IPP isomerases were combined to generate an almost complete model of the FMN-bound structure of the enzyme. In contrast to previous studies, positions of flexible loops were obtained and carefully analyzed by molecular dynamics. Docking simulations find a unique putative binding site for the IPP substrate.

UR - http://www.scopus.com/inward/record.url?scp=27744599634&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2005.10.114

DO - 10.1016/j.bbrc.2005.10.114

M3 - Article

AN - SCOPUS:27744599634

SN - 0006-291X

VL - 338

SP - 1515

EP - 1518

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 3

ER -

Structure of Thermus thermophilus type 2 isopentenyl diphosphate isomerase inferred from crystallography and molecular dynamics

Abstract

Access to Document

Other files and links

Fingerprint

Cite this