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dc.contributor.authorAl-Riyami, Bahjaen
dc.contributor.authorÜstok, Fatma Işıken
dc.contributor.authorStott, Katherineen
dc.contributor.authorChirgadze, Dimaen
dc.contributor.authorChristie, Grahamen
dc.date.accessioned2016-09-16T12:41:52Z
dc.date.available2016-09-16T12:41:52Z
dc.date.issued2016-08-02en
dc.identifier.issn0887-3585
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/260191
dc.description.abstract$\textit{Clostridium perfringens}$ spores employ two peptidoglycan lysins to degrade the spore cortex during germination. SleC initiates cortex hydrolysis to generate cortical fragments that are degraded further by the muramidase SleM. Here, we present the crystal structure of the $\textit{C. perfringens}$ S40 SleM protein at 1.8 Å. SleM comprises an N-terminal catalytic domain that adopts an irregular $\alpha/\beta$-barrel fold that is common to GH25 family lysozymes, plus a C-terminal fibronectin type III domain. The latter is involved in forming the SleM dimer that is evident in both the crystal structure and in solution. A truncated form of SleM that lacks the FnIII domain shows reduced activity against spore sacculi indicating that this domain may have a role in facilitating the position of substrate with respect to the enzyme’s active site.
dc.description.sponsorshipSultanate of Oman government (scholarship)
dc.languageEnglishen
dc.language.isoenen
dc.publisherWiley
dc.subjectcortex lytic enzymeen
dc.subjectpeptidoglycan lysinen
dc.subjectsporeen
dc.subjectGH25 familyen
dc.titleThe crystal structure of $\textit{Clostridium perfringens}$ SleM, a muramidase involved in cortical hydrolysis during spore germinationen
dc.typeArticle
dc.description.versionThis is the author accepted manuscript. The final version is available from Wiley via http://dx.doi.org/10.1002/prot.25112en
prism.publicationDate2016en
prism.publicationNameProteins: Structure, Function, and Bioinformaticsen
dc.identifier.doi10.17863/CAM.4424
dcterms.dateAccepted2016-07-25en
rioxxterms.versionofrecord10.1002/prot.25112en
rioxxterms.versionAMen
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserveden
rioxxterms.licenseref.startdate2016-08-02en
dc.contributor.orcidStott, Katherine [0000-0002-4014-1188]
dc.contributor.orcidChirgadze, Dima [0000-0001-9942-0993]
dc.contributor.orcidChristie, Graham [0000-0001-7177-9646]
dc.identifier.eissn1097-0134
rioxxterms.typeJournal Article/Reviewen
rioxxterms.freetoread.startdate2017-08-02


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