SASDDB6: Small glutamine-rich tetratricopeptide repeat-containing protein ...

基本情報

登録情報

データベース: SASBDB / ID: SASDDB6

試料

Small glutamine-rich tetratricopeptide repeat-containing protein alpha (full length; SGTA_FL)

• Small glutamine-rich tetratricopeptide repeat-containing protein alpha full length (protein), SGTA_FL, Homo sapiens

機能・相同性

分子機能:

TRC complex / negative regulation of ERAD pathway / tail-anchored membrane protein insertion into ER membrane / positive regulation of ERAD pathway / post-translational protein targeting to endoplasmic reticulum membrane / BAT3 complex binding / positive regulation of ubiquitin-dependent protein catabolic process / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / negative regulation of ubiquitin-dependent protein catabolic process / ERAD pathway / molecular adaptor activity / nucleoplasm / identical protein binding / nucleus / membrane / cytosol / cytoplasm

ドメイン・相同性:

SGTA, homodimerisation domain / Homodimerisation domain of SGTA / : / Tetratricopeptide repeat / Tetratricopeptide repeat / TPR repeat region circular profile. / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat / Tetratricopeptide-like helical domain superfamily

構成要素:

Small glutamine-rich tetratricopeptide repeat-containing protein alpha

• 生物種: Homo sapiens (ヒト)
• 引用: ジャーナル: BMC Biol / 年: 2018; タイトル: Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control.; 著者: Santiago Martínez-Lumbreras / Ewelina M Krysztofinska / Arjun Thapaliya / Alessandro Spilotros / Dijana Matak-Vinkovic / Enrico Salvadori / Peristera Roboti / Yvonne Nyathi / Janina H Muench / Maxie M Roessler / Dmitri I Svergun / Stephen High / Rivka L Isaacson / ; 要旨: BACKGROUND: Protein quality control mechanisms are essential for cell health and involve delivery of proteins to specific cellular compartments for recycling or degradation. In particular, stray hydrophobic proteins are captured in the aqueous cytosol by a co-chaperone, the small glutamine-rich, tetratricopeptide repeat-containing protein alpha (SGTA), which facilitates the correct targeting of tail-anchored membrane proteins, as well as the sorting of membrane and secretory proteins that mislocalize to the cytosol and endoplasmic reticulum-associated degradation. Full-length SGTA has an unusual elongated dimeric structure that has, until now, evaded detailed structural analysis. The C-terminal region of SGTA plays a key role in binding a broad range of hydrophobic substrates, yet in contrast to the well-characterized N-terminal and TPR domains, there is a lack of structural information on the C-terminal domain. In this study, we present new insights into the conformation and organization of distinct domains of SGTA and show that the C-terminal domain possesses a conserved region essential for substrate processing in vivo.; RESULTS: We show that the C-terminal domain region is characterized by α-helical propensity and an intrinsic ability to dimerize independently of the N-terminal domain. Based on the properties of different regions of SGTA that are revealed using cell biology, NMR, SAXS, Native MS, and EPR, we observe that its C-terminal domain can dimerize in the full-length protein and propose that this reflects a closed conformation of the substrate-binding domain.; CONCLUSION: Our results provide novel insights into the structural complexity of SGTA and provide a new basis for mechanistic studies of substrate binding and release at the C-terminal region.

登録者

• Rivka Isaacson (King's College London)

モデル

試料

• 試料: 名称: Small glutamine-rich tetratricopeptide repeat-containing protein alpha (full length; SGTA_FL); 試料濃度: 0.60-8.80
• バッファ: 名称: 10 mM potassium phosphate, 100 mM NaCl / pH: 6

要素 #1055

名称: SGTA_FL / タイプ: protein
記述: Small glutamine-rich tetratricopeptide repeat-containing protein alpha full length
分子量: 34.207 / 分子数: 2 / 由来: Homo sapiens / 参照: UniProt: O43765
配列:

GSMDNKKRLA YAIIQFLHDQ LRHGGLSSDA QESLEVAIQC LETAFGVTVE DSDLALPQTL PEIFEAAATG KEMPQDLRSP ARTPPSEEDS AEAERLKTEG NEQMKVENFE AAVHFYGKAI ELNPANAVYF CNRAAAYSKL GNYAGAVQDC ERAICIDPAY SKAYGRMGLA LSSLNKHVEA VAYYKKALEL DPDNETYKSN LKIAELKLRE APSPTGGVGS FDIAGLLNNP GFMSMASNLM NNPQIQQLMS GMISGGNNPL GTPGTSPSQN DLASLIQAGQ QFAQQMQQQN PELIEQLRSQ IRSRTPSASN DDQQE

実験情報

• ビーム: 設備名称: PETRA III EMBL P12 / 地域: Hamburg / 国: Germany / 線源: X-ray synchrotron / 波長: 0.124 Å / スペクトロメータ・検出器間距離: 3 mm
• 検出器: 名称: Pilatus 2M

スキャン

タイトル: Small glutamine-rich tetratricopeptide repeat-containing protein alpha (full length; SGTA_FL)
測定日: 2015年6月5日 / セル温度: 25 °C / 照射時間: 0.045 sec. / フレーム数: 20 / 単位: 1/nm /

	Min	Max
Q	0.0507	4.8012

結果

Experimental MW: 65 kDa / カーブのタイプ: merged

	Guinier	Guinier error
前方散乱 I0	16855	62
慣性半径, Rg	4.2 nm	0.1

	Min	Max
Guinier point	3	93