Resonance assignments and secondary structure prediction of secretory protein Rv0603 from Mycobacterium tuberculosis H37Rv
We report the NMR resonance assignments of N-terminal signal sequence deleted secretory protein Rv0603 (∆ 1–28 −Rv0603) from Mycobacterium tuberculosis H37Rv. ∆ 1–28 −Rv0603 displayed good peak yield and signal dispersion in 2D [ 15 N- 1 H] HSQC spectrum, which prompted us to proceed for resonance a...
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Published in | Biomolecular NMR assignments Vol. 14; no. 2; pp. 217 - 219 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
Dordrecht
Springer Netherlands
01.10.2020
Springer Nature B.V |
Subjects | |
Online Access | Get full text |
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Summary: | We report the NMR resonance assignments of N-terminal signal sequence deleted secretory protein Rv0603 (∆
1–28
−Rv0603) from
Mycobacterium tuberculosis
H37Rv. ∆
1–28
−Rv0603 displayed good peak yield and signal dispersion in 2D [
15
N-
1
H] HSQC spectrum, which prompted us to proceed for resonance assignments on this construct. Standard triple-resonance experiments for resonance assignments were recorded on [
U
-
15
N]-∆Rv0603 and [
U
-
15
N,
13
C]-∆Rv0603 samples. We obtained 97% of backbone
1
H
N
, 98% of
13
C
α
, 98% of
1
H
α
, 96% of
13
C´, 100% of
13
C
β
, 100% of
1
H
β
and 98% of side-chain
1
H chemical shifts. This protein does not show any sequence similarity to any other protein of known structure. Determination of its solution structure would facilitate understanding of its biological function. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1874-2718 1874-270X |
DOI: | 10.1007/s12104-020-09948-5 |