SASDDR6: The ferredoxin protease, FusC, E83A mutant (Ferredoxin protease E...

基本情報

登録情報

データベース: SASBDB / ID: SASDDR6

試料

The ferredoxin protease, FusC, E83A mutant

• Ferredoxin protease E83A mutant (protein), FusC E83A, Pectobacterium atrosepticum SCRI1043

機能・相同性

分子機能:

metalloendopeptidase activity / proteolysis / metal ion binding

ドメイン・相同性:

: / Peptidase M16, zinc-binding site / Insulinase family, zinc-binding region signature. / Peptidase M16, C-terminal / Peptidase M16 inactive domain / Peptidase M16, N-terminal / Insulinase (Peptidase family M16) / Metalloenzyme, LuxS/M16 peptidase-like

構成要素:

Zinc protease

• 生物種: Pectobacterium atrosepticum SCRI1043 (バクテリア)
• 引用: ジャーナル: PLoS Biol / 年: 2018; タイトル: FusC, a member of the M16 protease family acquired by bacteria for iron piracy against plants.; 著者: Rhys Grinter / Iain D Hay / Jiangning Song / Jiawei Wang / Don Teng / Vijay Dhanesakaran / Jonathan J Wilksch / Mark R Davies / Dene Littler / Simone A Beckham / Ian R Henderson / Richard A Strugnell / Gordon Dougan / Trevor Lithgow / ; 要旨: Iron is essential for life. Accessing iron from the environment can be a limiting factor that determines success in a given environmental niche. For bacteria, access of chelated iron from the environment is often mediated by TonB-dependent transporters (TBDTs), which are β-barrel proteins that form sophisticated channels in the outer membrane. Reports of iron-bearing proteins being used as a source of iron indicate specific protein import reactions across the bacterial outer membrane. The molecular mechanism by which a folded protein can be imported in this way had remained mysterious, as did the evolutionary process that could lead to such a protein import pathway. How does the bacterium evolve the specificity factors that would be required to select and import a protein encoded on another organism's genome? We describe here a model whereby the plant iron-bearing protein ferredoxin can be imported across the outer membrane of the plant pathogen Pectobacterium by means of a Brownian ratchet mechanism, thereby liberating iron into the bacterium to enable its growth in plant tissues. This import pathway is facilitated by FusC, a member of the same protein family as the mitochondrial processing peptidase (MPP). The Brownian ratchet depends on binding sites discovered in crystal structures of FusC that engage a linear segment of the plant protein ferredoxin. Sequence relationships suggest that the bacterial gene encoding FusC has previously unappreciated homologues in plants and that the protein import mechanism employed by the bacterium is an evolutionary echo of the protein import pathway in plant mitochondria and plastids.

登録者

• Grinter Grinter (Monash University, Melbourne, Australia)

モデル

試料

• 試料: 名称: The ferredoxin protease, FusC, E83A mutant / 試料濃度: 10 mg/ml
• バッファ: 名称: 20 mM Tris HCl, 150 nM NaCl, 0.02 % NaAzide, 5% Glycerol; pH: 7.8

要素 #1084

名称: FusC E83A / タイプ: protein / 記述: Ferredoxin protease E83A mutant / 分子量: 101.195 / 分子数: 1 / 由来: Pectobacterium atrosepticum SCRI1043 / 参照: UniProt: Q6D8U3
配列:

EEIKSPLPVF KEGTLANGFR YTLVQLEGPK TRVDIRLIVD VGSIDEKDNE SGVAHMVAHM VFRASDAFPQ GVSTELHKQG WGRGQSYNAV TNYERTMYMM SPPKGNLDLG ATLQALSQMT GHAKLLQSDL DDERKIILEE WRGKLGVAER MNQQRVQAIR HDSRYPSRPV IGTEESINDT PASVLQDFYQ RWYHPSNMRL MIIGDITPAD AEREIQRYFA ALPNVAVPTR DYYEPLLKPQ LKVARLQDSQ SGSSQVSFVY RFNDKDAFGQ SEYRHRLLTQ ITMSAVTRQV RRQKAELPQD ASSLVVRKSD IGKTTAALGF FANVMPGGHD AAISAVLKEI ERFKRYPLNE QDITEITSDI REVAQRMSVT PETREFADWV QQLTIVWQQD RPYVGSQQRG KDALEALDTI KGEDVNRHWQ RWLASPDTLA QFSVPGATPF TLPKPDAISK LQKQWALATL APLRLEEKKI IPELPSVTQS GKRTAVKTFA AQKVEQWQLS NGDRVVWLRA PEAGKKVYLT ATSQAGFMAT AMNPWQAQLA SQLVNQSGPA TWSGESLSNW KKEKTLSLSI DQEADQLTLS GTAPTEQLAS LFGLYRELNV APGIDPDVMK ESMMSLARQK ANDDQSVGGK RASEMTKLRF GEPAWQQPEI AELKKISAPA LLSQWHKAAS APVTYYLIAD MPATQLLPQV ERYLATIPRQ PASEVKQHLA LSGKREATSA INVEPRADIL TWSFTPHAWT PQAAVQVSIA RNIASKYLKT SLRDDALGIY RMRVDSELED KKQRIETEVS FTSAPERAQE LWTLAEQAFS ELPTKITQQD VDEQKAQFIR AEKGRQGDLT TIQRRLILSY RHYNDPRYLS NASKLADSIT LESVRAMSAK LYNPDNRVLY ITLPQEVKE

実験情報

• ビーム: 設備名称: Australian Synchrotron SAXS/WAXS / 地域: Melbourne / 国: Australia / 形状: Point / 線源: X-ray synchrotron / 波長: 0.103 Å / スペクトロメータ・検出器間距離: 2.68 mm
• 検出器: 名称: Pilatus 1M / Pixsize x: 172 mm

スキャン

タイトル: The ferredoxin protease FusC, E83A mutant / 測定日: 2017年4月6日 / 保管温度: 20 °C / セル温度: 20 °C / 単位: 1/A /

	Min	Max
Q	0.0064	0.279

距離分布関数 P(R)

ソフトウェア P(R): GNOM 5.0 / ポイント数: 533 /

	Min	Max
Q	0.00917184	0.216704
P(R) point	1	533
R	0	127

結果

カーブのタイプ: sec
コメント: Additional SEC parameters: Column type: GE Healthcare Superdex S200 10/300; Flow rate: 0.4 ml/min; Sample injection concentration: 10 mg/ml; Injection volume: 100 µl.

	実験値	Porod
分子量	100 kDa	89 kDa
体積	-	151.5 nm3

	P(R)	Guinier	Guinier error
前方散乱 I0	0.1299	0.13	0.00012
慣性半径, Rg	3.73 nm	3.69 nm	0.013

	Min	Max
D	-	12.7
Guinier point	8	74