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Structure of a fatt...
Structure of a fatty-acid-binding protein from Bacillus subtilis determined by sulfur-SAD phasing using in-house chromium radiation
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- Nan, Jie (författare)
- Lund University,Lunds universitet,MAX IV-laboratoriet,MAX IV Laboratory,Peking University
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Zhou, Yanfeng (författare)
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Yang, Cheng (författare)
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Brostromer, Erik (författare)
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Kristensen, Ole (författare)
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- Su, Xiao Dong (författare)
- Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
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(creator_code:org_t)
- 2009
- 2009
- Engelska 9 s.
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Ingår i: Acta Crystallographica. Section D: Biological Crystallography. - 1399-0047. ; 65:Pt 5, s. 8-440
- Relaterad länk:
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http://dx.doi.org/10...
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https://lup.lub.lu.s...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- Sulfur single-wavelength anomalous dispersion (S-SAD) and halide-soaking methods are increasingly being used for ab initio phasing. With the introduction of in-house Cr X-ray sources, these methods benefit from the enhanced anomalous scattering of S and halide atoms, respectively. Here, these methods were combined to determine the crystal structure of BsDegV, a DegV protein-family member from Bacillus subtilis. The protein was cocrystallized with bromide and low-redundancy data were collected to 2.5 A resolution using Cr Kalpha radiation. 17 heavy-atom sites (ten sulfurs and seven bromides) were located using standard methods. The anomalous scattering of some of the BsDegV S atoms and Br atoms was weak, thus neither sulfurs nor bromides could be used alone for structure determination using the collected data. When all 17 heavy-atom sites were used for SAD phasing, an easily interpretable electron-density map was obtained after density modification. The model of BsDegV was built automatically and a palmitate was found tightly bound in the active site. Sequence alignment and comparisons with other known DegV structures provided further insight into the specificity of fatty-acid selection and recognition within this protein family.
Nyckelord
- Amino Acid Sequence
- Bacillus subtilis
- Bacterial Proteins
- Binding Sites
- Bromides
- Chromium
- Crystallography, X-Ray
- Models, Molecular
- Molecular Sequence Data
- Palmitates
- Protein Conformation
- Recombinant Fusion Proteins
- Sequence Alignment
- Sequence Homology, Amino Acid
- Sulfur
Publikations- och innehållstyp
- art (ämneskategori)
- ref (ämneskategori)
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