Structural Analysis of Papain-Like NlpC/P60 Superfamily Enzymes with a Circularly Permuted Topology Reveals Potential Lipid Binding Sites-Reference-Cited by-同舟云学术

Structural Analysis of Papain-Like NlpC/P60 Superfamily Enzymes with a Circularly Permuted Topology Reveals Potential Lipid Binding Sites

Published:2011-07-22 Issue:7 Volume:6 Page:e22013
ISSN:1932-6203
Container-title:PLoS ONE
language:en
Short-container-title:PLoS ONE

Author:

Xu Qingping,Rawlings Neil D.,Chiu Hsiu-Ju,Jaroszewski Lukasz,Klock Heath E.,Knuth Mark W.,Miller Mitchell D.,Elsliger Marc-Andre,Deacon Ashley M.,Godzik Adam,Lesley Scott A.,Wilson Ian A.

Publisher

Public Library of Science (PLoS)

Subject

Multidisciplinary

Reference40 articles.

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4. Dual binding sites for translocation catalysis by Escherichia coli glutathionylspermidine synthetase.;CH Pai;EMBO J,2006

5. Structure of the γ-D-glutamyl-L-diamino acid endopeptidase YkfC from Bacillus cereus in complex with L-Ala-γ-D-Glu: insights into substrate recognition by NlpC/P60 cysteine peptidases.;Q Xu;Acta Crystallogr Sect F Struct Biol Cryst Commun,2010

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