Journal article

Crystal structure of an intracellular subtilisin reveals novel structural features unique to this subtilisin family

Abstract:: The intracellular subtilisin proteases (ISPs) are the only known members of the important and ubiquitous subtilisin family that function exclusively within the cell, constituting a major component of the degradome in many Gram-positive bacteria. The first ISP structure reported herein at a spacing of 1.56 Å reveals features unique among subtilisins that has enabled potential functional and physiological roles to be assigned to sequence elements exclusive to the ISPs. Unlike all other subtilis...
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Publication status:: Published

Peer review status:: Peer reviewed

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APA Style

Vévodová, J., Gamble, M., Künze, G., Ariza, A., Dodson, E., Jones, D., & Wilson, K. (2010). Crystal structure of an intracellular subtilisin reveals novel structural features unique to this subtilisin family. Structure, 18(6), 744–755.

MLA Style

Vévodová, J., et al. “Crystal Structure of an Intracellular Subtilisin Reveals Novel Structural Features Unique to This Subtilisin Family.” Structure, vol. 18, no. 6, Cell Press, 2010, pp. 744–55.

Chicago Style

Vévodová, J, M Gamble, G Künze, A Ariza, E Dodson, D Jones, and K Wilson. 2010. “Crystal Structure of an Intracellular Subtilisin Reveals Novel Structural Features Unique to This Subtilisin Family.” Structure 18 (6): 744–55.
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Publisher copy:: 10.1016/j.str.2010.03.008

Authors

+ Vévodová, J More by this author

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+ Gamble, M More by this author

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+ Künze, G More by this author

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+ Ariza, A More by this author

Institution:

University of Oxford

Division:

MSD

Department:

Pathology Dunn School

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+ Dodson, E More by this author

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Bibliographic Details

Publisher:: Cell Press
Journal:: Structure More from this journal
Volume:: 18
Issue:: 6
Pages:: 744-755
Publication date:: 2010-06-09
DOI:: 10.1016/j.str.2010.03.008
EISSN:: 1878-4186
ISSN:: 0969-2126
Pmid:: 20541512

Item Description

Language:: English
Keywords:: SBTMR
Pubs id:: pubs:659857
UUID:: uuid:2a51a97e-7775-4184-9f03-d01fd4219de8
Local pid:: pubs:659857
Source identifiers:: 659857
Deposit date:: 2016-12-13

Terms of use

Copyright holder:: Elsevier Ltd
Copyright date:: 2010
Notes:: Copyright © 2010 Elsevier Ltd.

Licence:: Terms and Conditions of Use for Oxford University Research Archive

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