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Structure paper

TitleStructure of the peptidoglycan polymerase RodA resolved by evolutionary coupling analysis.
Journal, issue, pagesNature, Vol. 556, Page 118-121, Year 2018
Publish dateOct 15, 2017 (structure data deposition date)
AuthorsSjodt, M. / Brock, K. / Dobihal, G. / Rohs, P.D.A. / Green, A.G. / Hopf, T.A. / Meeske, A.J. / Srisuknimit, V. / Kahne, D. / Walker, S. ...Sjodt, M. / Brock, K. / Dobihal, G. / Rohs, P.D.A. / Green, A.G. / Hopf, T.A. / Meeske, A.J. / Srisuknimit, V. / Kahne, D. / Walker, S. / Marks, D.S. / Bernhardt, T.G. / Rudner, D.Z. / Kruse, A.C.
External linksNature / PubMed:29590088
MethodsX-ray diffraction
Resolution2.908 - 3.194 Å
Structure data

PDB-6bar:
Crystal structure of Thermus thermophilus Rod shape determining protein RodA (Q5SIX3_THET8)
Method: X-RAY DIFFRACTION / Resolution: 2.908 Å

PDB-6bas:
Crystal structure of Thermus thermophilus Rod shape determining protein RodA D255A mutant (Q5SIX3_THET8)
Method: X-RAY DIFFRACTION / Resolution: 3.194 Å

Chemicals

ChemComp-OLC:
(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

Source
  • thermus thermophilus (strain hb8 / atcc 27634 / dsm 579) (bacteria)
KeywordsTRANSFERASE / Peptidoglycan Glycosyltransferase / transmembrane protein / Shape Elogation Division and Sporulation / elongasome

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