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TitleStructure and cooperativity of a T-state mutant of histidine decarboxylase from Lactobacillus 30a.
Journal, issue, pagesProteins, Vol. 46, Page 321-329, Year 2002
Publish dateMar 29, 2001 (structure data deposition date)
AuthorsWorley, S. / Schelp, E. / Monzingo, A.F. / Ernst, S. / Robertus, J.D.
External linksProteins / PubMed:11835507
MethodsX-ray diffraction
Resolution2.5 - 3.2 Å
Structure data

PDB-1ibt:
STRUCTURE OF THE D53,54N MUTANT OF HISTIDINE DECARBOXYLASE AT-170 C
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-1ibu:
STRUCTURE OF THE D53,54N MUTANT OF HISTIDINE DECARBOXYLASE AT 25 C
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

PDB-1ibv:
STRUCTURE OF THE D53,54N MUTANT OF HISTIDINE DECARBOXYLASE BOUND WITH HISTIDINE METHYL ESTER AT-170 C
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-1ibw:
STRUCTURE OF THE D53,54N MUTANT OF HISTIDINE DECARBOXYLASE BOUND WITH HISTIDINE METHYL ESTER AT 25 C
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-PVH:
HISTIDINE-METHYL-ESTER / inhibitor*YM

Source
  • lactobacillus sp. (bacteria)
  • lactobacillus sp. 30a (bacteria)
KeywordsLYASE / HELIX DISORDER / LESS ACTIVE FORM / SITE-DIRECTED MUTANT / PYRUVOYL / CARBOXY-LYASE / SUBSTRATE-INDUCED ACTIVATION / ACTIVE FORM

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