1RWI

Extracellular domain of Mycobacterium tuberculosis PknD

1RWI の概要

• エントリーDOI: 10.2210/pdb1rwi/pdb
• 関連するPDBエントリー: 1RWL
• 分子名称: Serine/threonine-protein kinase pknD, CADMIUM ION (3 entities in total)
• 機能のキーワード: beta propeller, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc, transferase
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 58612.67

構造登録者

Good, M.C.,Greenstein, A.E.,Young, T.A.,Ng, H.L.,Alber, T.,TB Structural Genomics Consortium (TBSGC) (登録日: 2003-12-16, 公開日: 2004-04-27, 最終更新日: 2024-02-14)

主引用文献

Good, M.C.,Greenstein, A.E.,Young, T.A.,Ng, H.L.,Alber, T.
Sensor Domain of the Mycobacterium tuberculosis Receptor Ser/Thr Protein Kinase, PknD, forms a Highly Symmetric beta Propeller.
J.Mol.Biol., 339:459-469, 2004

PubMed Abstract: Diverse pathogenic bacteria produce transmembrane receptor Ser/Thr protein kinases (STPKs), but little is known about the signals mediated by these "eukaryotic-like" proteins. To explore the basis for signaling in the bacterial STPK receptor family, we determined the structure of the sensor domain of Mycobacterium tuberculosis PknD. In two crystal forms, the PknD sensor domain forms a rigid, six-bladed beta-propeller with a flexible tether to the transmembrane domain. The PknD sensor domain is the most symmetric beta-propeller structure described. All residues that vary most among the blade subdomains cluster in the large "cup" motif, analogous to the ligand-binding surface in many beta-propeller proteins. These results suggest that PknD binds a multivalent ligand that signals by changing the quaternary structure of the intracellular kinase domain.

PubMed: 15136047
DOI: 10.1016/j.jmb.2004.03.063

実験手法

X-RAY DIFFRACTION (1.8 Å)