Articles by Matthias Haffke in JoVE
Den MultiBac Protein Complex produksjonsplattform på EMBL Imre Berger1, Frederic Garzoni1, Maxime Chaillet1, Matthias Haffke1, Kapil Gupta1, Alice Aubert1 1EMBL Grenoble Outstation and Unit of Virus Host Cell Interactions (UVHCI) UMR5322 Protein komplekser katalysere viktige cellulære funksjoner. Detaljert funksjonell og strukturell karakterisering av mange essensielle komplekser krever rekombinant produksjon. MultiBac er en Baculovirus / insekt celle system spesielt skreddersydd for å uttrykke eukaryote proteiner og deres komplekser. MultiBac ble gjennomført som en åpen tilgang plattform, og standard operasjonsprosedyrer utviklet for å maksimere sin nytte.
Other articles by Matthias Haffke on PubMed
Structures of the Nucleotide-binding Domain of the Human ABCB6 Transporter and Its Complexes with Nucleotides Acta Crystallographica. Section D, Biological Crystallography. Sep, 2010 | Pubmed ID: 20823549 The human ATP-binding cassette (ABC) transporter ABCB6 is involved in haem-precursor transport across the mitochondrial membrane. The crystal structure of its nucleotide-binding domain (NBD) has been determined in the apo form and in complexes with ADP, with ADP and Mg(2+) and with ATP at high resolution. The overall structure is L-shaped and consists of two lobes, consistent with other reported NBD structures. Nucleotide binding is mediated by the highly conserved Tyr599 and the Walker A motif, and induces notable structural changes. Structural comparison with other structurally characterized NBDs and full-length ABC transporters gives the first insight into the possible catalytic mechanism of ABCB6 and the role of the N-terminal helix alpha(1) in full-length ABCB6.
Structure of the Effector-binding Domain of the LysR-type Transcription Factor RovM from Yersinia Pseudotuberculosis Acta Crystallographica. Section D, Biological Crystallography. Feb, 2011 | Pubmed ID: 21245528 In enteropathogenic Yersinia, the expression of several early-phase virulence factors such as invasin is tightly regulated in response to environmental cues. The responsible regulatory network is complex, involving several regulatory RNAs and proteins such as the LysR-type transcription regulator (LTTR) RovM. In this study, the crystal structure of the effector-binding domain (EBD) of RovM, the first LTTR protein described as being involved in virulence regulation, was determined at a resolution of 2.4â€…Ã…. Size-exclusion chromatography and comparison with structures of full-length LTTRs show that RovM is most likely to adopt a tetrameric arrangement with two distant DNA-binding domains (DBDs), causing the DNA to bend around it. Additionally, a cavity was detected in RovM which could bind small inducer molecules.