Interplay between an AAA module and an integrin I domain may regulate the function of magnesium chelatase
- 1 August 2001
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 311 (1) , 111-122
- https://doi.org/10.1006/jmbi.2001.4834
Abstract
No abstract availableKeywords
This publication has 51 references indexed in Scilit:
- Structural and mechanistic basis of porphyrin metallation by ferrochelataseJournal of Molecular Biology, 2000
- Common Chelatase Design in the Branched Tetrapyrrole Pathways of Heme and Anaerobic Cobalamin SynthesisBiochemistry, 1999
- ATPase activity associated with the magnesium-protoporphyrin IX chelatase enzyme of Synechocystis PCC6803: evidence for ATP hydrolysis during Mg2+ insertion, and the MgATP-dependent interaction of the ChlI and ChlD subunitsBiochemical Journal, 1999
- The hexamerization domain of N-ethylmaleimide-sensitive factor: structural clues to chaperone functionStructure, 1999
- Heterologous Expression of the Rhodobacter capsulatus BchI, -D, and -H Genes That Encode Magnesium Chelatase Subunits and Characterization of the Reconstituted EnzymePublished by Elsevier ,1998
- CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choiceNucleic Acids Research, 1994
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Directed Mutational Analysis of Bacteriochlorophyll a Biosynthesis in Rhodobacter capsulatusJournal of Molecular Biology, 1994
- A Superfamily of ATPases with Diverse Functions Containing Either Classical or Deviant ATP-binding MotifJournal of Molecular Biology, 1993
- Integrins: Versatility, modulation, and signaling in cell adhesionCell, 1992