Abstract

Doc number: 379

Abstract

Background: Enzyme active sites can be connected to the exterior environment by one or more channels passing through the protein. Despite our current knowledge of enzyme structure and function, surprisingly little is known about how often channels are present or about any structural features such channels may have in common.

Results: Here, we analyze the long channels (i.e. >15 Å) leading to the active sites of 4,306 enzyme structures. We find that over 64% of enzymes contain two or more long channels, their typical length being 28 Å. We show that amino acid compositions of the channel significantly differ both to the composition of the active site, surface and interior of the protein.

Conclusions: The majority of enzymes have buried active sites accessible via a network of access channels. This indicates that enzymes tend to have buried active sites, with channels controlling access to, and egress from, them, and that suggests channels may play a key role in helping determine enzyme substrate.

Details

Title
Anatomy of enzyme channels
Author
Pravda, Lukás; Berka, Karel; Svobodová Vareková, Radka; Sehnal, David; Banás, Pavel; Laskowski, Roman A; Koca, Jaroslav; Otyepka, Michal
Publication year
2014
Publication date
2014
Publisher
BioMed Central
e-ISSN
14712105
Source type
Scholarly Journal
Language of publication
English
ProQuest document ID
1628381406
Copyright
© 2014 Pravda et al.; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.