Journal article icon

Journal article

A molecular dynamics investigation of mono and dimeric states of the outer membrane enzyme OMPLA.

Abstract:

OMPLA is a phospholipase found in the outer membranes of many Gram-negative bacteria. Enzyme activation requires calcium-induced dimerisation plus bilayer perturbation. As the conformation of OMPLA in the different crystal forms (monomer versus dimer; with/without bound Ca(2+)) is remarkably similar we have used multi-nanosecond molecular dynamics (MD) simulations to probe possible differences in conformational dynamics that may be related to enzyme activation. Simulations of calcium-free mon...

Expand abstract
Publication status:
Published

Actions


Access Document


Journal:
Journal of molecular biology More from this journal
Volume:
331
Issue:
1
Pages:
177-189
Publication date:
2003-08-01
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
Language:
English
Keywords:
Pubs id:
pubs:100922
UUID:
uuid:b63e843a-3a17-4a94-a24d-38277c7e7878
Local pid:
pubs:100922
Source identifiers:
100922
Deposit date:
2012-12-19

Terms of use


Views and Downloads






If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP