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Structure paper

TitleAtomic-resolution Crystal Structure of the Proteolytic Domain of Archaeoglobus fulgidus Lon Reveals the Conformational Variability in the Active Sites of Lon Proteases
Journal, issue, pagesJ. Mol. Biol., Vol. 351, Page 144-157, Year 2005
Publish dateMar 1, 2005 (structure data deposition date)
AuthorsBotos, I. / Melnikov, E.E. / Cherry, S. / Kozlov, S. / Makhovskaya, O.V. / Tropea, J.E. / Gustchina, A. / Rotanova, T.V. / Wlodawer, A.
External linksJ. Mol. Biol. / PubMed:16002085
MethodsX-ray diffraction
Resolution1.2 - 2.27 Å
Structure data

PDB-1z0b:
Crystal Structure of A. fulgidus Lon proteolytic domain E506A mutant
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

PDB-1z0c:
Crystal Structure of A. fulgidus Lon proteolytic domain D508A mutant
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

PDB-1z0e:
Crystal Structure of A. fulgidus Lon proteolytic domain
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

PDB-1z0g:
Crystal Structure of A. fulgidus Lon proteolytic domain
Method: X-RAY DIFFRACTION / Resolution: 2.27 Å

PDB-1z0w:
Crystal Structure of A. fulgidus Lon proteolytic domain at 1.2A resolution
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

Source
  • archaeoglobus fulgidus (archaea)
KeywordsHYDROLASE / ATP-DEPENDENT PROTEASE / CATALYTIC SER-LYS DYAD / B-type Lon / 'ATP-DEPENDENT PROTEASE / B-type Lon'

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