SASDD53: Tetratrico peptide repeat domain of Bacterial cellulose synthesis...

Basic information

• Entry: Database: SASBDB / ID: SASDD53

Sample

Tetratrico peptide repeat domain of Bacterial cellulose synthesis subunit C

• Bacterial cellulose synthesis subunit C (protein), BcsC-TPR, Enterobacter sp. CJF-002

Function / homology

Function:

cellulose biosynthetic process / outer membrane

Domain/homology:

Cellulose synthase operon C, C-terminal / Cellulose synthase operon protein C C-terminus (BCSC_C) / : / Tetratricopeptide repeat / Tetratricopeptide repeat / Tetratricopeptide repeat / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat / Tetratricopeptide-like helical domain superfamily

Component:

Cellulose synthase subunit C

• Biological species: Enterobacter sp. CJF-002 (bacteria)
• Citation: Journal: Sci Rep / Year: 2017; Title: Crystal structure of the flexible tandem repeat domain of bacterial cellulose synthesis subunit C.; Authors: Shingo Nojima / Ayumi Fujishima / Koji Kato / Kayoko Ohuchi / Nobutaka Shimizu / Kento Yonezawa / Kenji Tajima / Min Yao / ; Abstract: Bacterial cellulose (BC) is synthesized and exported through the cell membrane via a large protein complex (terminal complex) that consists of three or four subunits. BcsC is a little-studied subunit considered to export BC to the extracellular matrix. It is predicted to have two domains: a tetratrico peptide repeat (TPR) domain and a β-barrelled outer membrane domain. Here we report the crystal structure of the N-terminal part of BcsC-TPR domain (Asp24-Arg272) derived from Enterobacter CJF-002. Unlike most TPR-containing proteins which have continuous TPR motifs, this structure has an extra α-helix between two clusters of TPR motifs. Five independent molecules in the crystal had three different conformations that varied at the hinge of the inserted α-helix. Such structural feature indicates that the inserted α-helix confers flexibility to the chain and changes the direction of the TPR super-helix, which was also suggested by structural analysis of BcsC-TPR (Asp24-Leu664) in solution by size exclusion chromatography-small-angle X-ray scattering. The flexibility at the α-helical hinge may play important role for exporting glucan chains.

Contact author

• Kento Yonezawa (High Energy Accelerater Research Organization)

Models

• Model #1746: ; Type: dummy / Software: (ATSAS 2.7) / Radius of dummy atoms: 4.25 A / Symmetry: P1 / Chi-square value: 1.906 / P-value: 0.000126; Search similar-shape structures of this assembly by Omokage search (details)

Sample

• Sample: Name: Tetratrico peptide repeat domain of Bacterial cellulose synthesis subunit C; Specimen concentration: 0.71-1.80
• Buffer: Name: 50 mM HEPES, 100 mM KCl / pH: 8

Entity #947

Name: BcsC-TPR / Type: protein / Description: Bacterial cellulose synthesis subunit C / Formula weight: 71.298 / Num. of mol.: 1 / Source: Enterobacter sp. CJF-002 / References: UniProt: K0J1W8
Sequence:

GHMDEPTAQQ QLLSQVRLGE ATKREDLVRQ SLYRLELIDP DNPDVIAARF RYLLRQGDNA GAQKQLDRMK QLAPDSAAYK SSVTSMTLSG AEGRQALQQA RLQATTGHVP EALAAYDALF KGNPPEGDLA VEYWALVAKV PARRSEAITQ LKALNARNPG NAALQNSLAQ LLFGEGRDAE AYAVLEQMAK SSAGREAAAG LWYQQIQRMP VSDASVKALQ RFLTVFSSGD TVDSARTQLA AQQKQLADPA FRARATGLAA VDAGQGAKAV NELRQAVNAN GTDSEAVGAL GQAYSQSGDR ARAVAQFEKA IAMDPTSGNR SKWDSLLKTN RYWLLIQQGD AALKANNPGE AERLYSQARR IDNTDSYAVL GLGDAAMARK DSHAAESFYR QALRMDSGNS NAVRGLANIY RARSPQEADT FIQSLSASQR RSIDDIERGL KNDRLAQQAE ALENSGQWAQ AAELQRQRLA LDPGSVWVTY RLASDLRQAG EPREADAHMQ RLAALKPGDP EQVYAYGLYL SGNNQEMAAL NQLNALPKAQ WNSNIQELAE RLQTNRLLDN ANRLRDSGHE EQARALLAQQ PASTRIDLTL ADWAQQGGDS ASAQHYFNRV LEREPNNQDA LLGLAELYAA DGNKMAARAQ LAKLLEHHHH HH

Experimental information

• Beam: Instrument name: Photon Factory (PF), High Energy Acceleration Research Organization (KEK) BL-10C; City: Tsukuba / 国: Japan / Type of source: X-ray synchrotron / Wavelength: 0.1 Å / Dist. spec. to detc.: 2.01 mm
• Detector: Name: Pilatus3 2M / Pixsize x: 0.172 mm

Scan

Title: Tetratrico peptide repeat domain of Bacterial cellulose synthesis subunit C
Measurement date: Apr 24, 2017 / Storage temperature: 20 °C / Cell temperature: 20 °C / Exposure time: 20 sec. / Number of frames: 28 / Unit: 1/A /

	Min	Max
Q	0.0083	0.4001

Distance distribution function P(R)

Sofotware P(R): GNOM 5.0 / Number of points: 550 /

	Min	Max
Q	0.00860043	0.156115
P(R) point	1	550
R	0	185.3

Result

Type of curve: extrapolated

	Experimental	Standard	Standard error	Porod
MW	73.4 kDa	73.4 kDa	0.5	72.1 kDa
Volume	-	-	-	115.3 nm3

	P(R)	P(R) error	Guinier	Guinier error
Forward scattering, I0	0.1035	0.0003	0.105	0.0004
Radius of gyration, Rg	5.13 nm	0.02	5.12 nm	0.08

	Min	Max
D	-	18.53
Guinier point	2	59