1JYA

Crystal Structure of SycE

Summary for 1JYA

• Entry DOI: 10.2210/pdb1jya/pdb
• Descriptor: YOPE regulator (2 entities in total)
• Functional Keywords: specific chaperone, type iii secretion, chaperone
• Biological source: Yersinia pseudotuberculosis
• Total number of polymer chains: 2
• Total formula weight: 29600.46

Authors

Ghosh, P.,Birtalan, S. (deposition date: 2001-09-11, release date: 2001-10-31, Last modification date: 2024-10-30)

Primary citation

Birtalan, S.,Ghosh, P.
Structure of the Yersinia type III secretory system chaperone SycE.
Nat.Struct.Biol., 8:974-978, 2001

PubMed Abstract: In the type III secretory system of bacterial pathogens, a large number of sequence-divergent but characteristically small (approximately 14-19 kDa), acidic (pI approximately 4-5) chaperone proteins have been identified. We present the 1.74 A resolution crystal structure of the Yersinia pseudotuberculosis chaperone SycE, whose action in promoting translocation of YopE into host macrophages is essential to Yersinia pathogenesis. SycE, a compact, globular dimer with a novel fold, has two large hydrophobic surface patches that may form binding sites for YopE or other type III components. These patches are formed by structurally key residues that are conserved among many chaperones, suggesting shared structural and functional relationships. A negative electrostatic potential covers almost the entire surface of SycE and is likely conserved in character, but not in detail, among chaperones. The structure provides the first structural insights into possible modes of action of SycE and type III chaperones in general.

PubMed: 11685245
DOI: 10.1038/nsb1101-974

Experimental method

X-RAY DIFFRACTION (1.74 Å)