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Structure of the N-...
Structure of the N-terminal domain of the metalloprotease PrtV from Vibrio cholerae
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- Edwin, Aaron (författare)
- Umeå universitet,Kemiska institutionen,Umeå Centre for Microbial Research (UCMR)
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- Persson, Cecilia, 1974 (författare)
- Gothenburg University,Göteborgs universitet,Svenskt NMR-centrum vid Göteborgs universitet,Swedish NMR Centre at Göteborg University
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- Mayzel, Maxim (författare)
- Gothenburg University,Göteborgs universitet,Svenskt NMR-centrum vid Göteborgs universitet,Swedish NMR Centre at Göteborg University
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- Wai, Sun Nyunt (författare)
- Umeå universitet,Molekylär Infektionsmedicin, Sverige (MIMS),Institutionen för molekylärbiologi (Medicinska fakulteten),Umeå Centre for Microbial Research (UCMR)
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- Öhman, Anders (författare)
- Umeå universitet,Klinisk neurovetenskap
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- Karlsson, B Göran, 1962 (författare)
- Gothenburg University,Göteborgs universitet,Svenskt NMR-centrum vid Göteborgs universitet,Swedish NMR Centre at Göteborg University
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- Sauer-Eriksson, A. Elisabeth (författare)
- Umeå universitet,Umeå Centre for Microbial Research (UCMR),Kemiska institutionen
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(creator_code:org_t)
- 2015-11-06
- 2015
- Engelska.
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Ingår i: Protein Science. - : Wiley. - 0961-8368 .- 1469-896X. ; 24:12, s. 2076-2080
- Relaterad länk:
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https://onlinelibrar...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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https://gup.ub.gu.se...
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Abstract
Ämnesord
Stäng
- The metalloprotease PrtV from Vibrio cholerae serves an important function for the ability of bacteria to invade the mammalian host cell. The protein belongs to the family of M6 proteases, with a characteristic zinc ion in the catalytic active site. PrtV constitutes a 918 amino acids (102 kDa) multidomain pre-pro-protein that undergoes several N- and C-terminal modifications to form a catalytically active protease. We report here the NMR structure of the PrtV N- terminal domain (residues 23-103) that contains two short alpha-helices in a coiled coil motif. The helices are held together by a cluster of hydrophobic residues. Approximately 30 residues at the C-terminal end, which were predicted to form a third helical structure, are disordered. These residues are highly conserved within the genus Vibrio, which suggests that they might be functionally important.
Ämnesord
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Mikrobiologi inom det medicinska området (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Microbiology in the medical area (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Cell- och molekylärbiologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Cell and Molecular Biology (hsv//eng)
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Nyckelord
- Vibrio cholera
- metalloproteases
- PrtV
- N-terminal domain
- NMR
- LAGLIO F
- 1995
- JOURNAL OF BIOMOLECULAR NMR
- V6
- P277 inoda Sumio
- 2011
- BIOCONTROL SCIENCE
- V16
- P1 lm L.
- 2008
- BIOINFORMATICS
- V24
- P2780 itkevicius Karolis
- 2008
- FEBS JOURNAL
- V275
- P3167 itkevicius K
- 2006
- PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES
- Vibrio cholera
- metalloproteases
- PrtV
- N-terminal domain
- NMR
- purification
- expression
- software
- server
- Biochemistry & Molecular Biology
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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