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Structure paper

TitleMutational and structural study of RipA, a key enzyme in Mycobacterium tuberculosis cell division: evidence for the L-to-D inversion of configuration of the catalytic cysteine.
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 70, Page 2295-2300, Year 2014
Publish dateApr 14, 2014 (structure data deposition date)
AuthorsSqueglia, F. / Ruggiero, A. / Romano, M. / Vitagliano, L. / Berisio, R.
External linksActa Crystallogr. ,Sect. D / PubMed:25195744
MethodsX-ray diffraction
Resolution0.97 - 1.63 Å
Structure data

PDB-4q4g:
Structure of the Resuscitation Promoting Factor Interacting protein RipA mutated at C383
Method: X-RAY DIFFRACTION / Resolution: 0.97 Å

PDB-4q4n:
Structure of the Resuscitation Promoting Factor Interacting protein RipA mutated at H432
Method: X-RAY DIFFRACTION / Resolution: 1.38 Å

PDB-4q4t:
Structure of the Resuscitation Promoting Factor Interacting protein RipA mutated at E444
Method: X-RAY DIFFRACTION / Resolution: 1.63 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-FMT:
FORMIC ACID

ChemComp-GOL:
GLYCEROL

Source
  • mycobacterium tuberculosis (bacteria)
KeywordsHYDROLASE / alpha-beta / cell wall hydrolase / alpha beta

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