PDBsum entry 1vq0

Chaperone

PDB id: 1vq0

Contents

Protein chains

290 a.a. *

Ligands

UNL ×2

EDO ×3

Metals

_ZN ×2

_CL ×2

Waters ×273

* Residue conservation analysis

PDB id:

1vq0

Name:

Chaperone

Title:

Crystal structure of 33 kda chaperonin (heat shock protein 33 homolog) (hsp33) (tm1394) from thermotoga maritima at 2.20 a resolution

Structure:

33 kda chaperonin. Chain: a, b. Synonym: heat shock protein 33 homolog, hsp33. Engineered: yes

Source:

Thermotoga maritima. Organism_taxid: 2336. Gene: hslo, tm1394. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PQS)

Resolution:

2.20Å R-factor: 0.200 R-free: 0.241

Authors:

Joint Center For Structural Genomics (Jcsg)

Key ref:

L.Jaroszewski et al. (2005). Crystal structure of Hsp33 chaperone (TM1394) from Thermotoga maritima at 2.20 A resolution. Proteins, 61, 669-673. PubMed id: 16167343 DOI: 10.1002/prot.20542

Date:

30-Nov-04 Release date: 14-Dec-04

Protein chains

Q9X1B4  (HSLO_THEMA) -  33 kDa chaperonin from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

Seq: 290 a.a.

Struc: 290 a.a.

DOI no: 10.1002/prot.20542

Proteins 61:669-673 (2005)

PubMed id: 16167343

Crystal structure of Hsp33 chaperone (TM1394) from Thermotoga maritima at 2.20 A resolution.

L.Jaroszewski, R.Schwarzenbacher, D.McMullan, P.Abdubek, S.Agarwalla, E.Ambing, H.Axelrod, T.Biorac, J.M.Canaves, H.J.Chiu, A.M.Deacon, M.DiDonato, M.A.Elsliger, A.Godzik, C.Grittini, S.K.Grzechnik, J.Hale, E.Hampton, G.W.Han, J.Haugen, M.Hornsby, H.E.Klock, E.Koesema, A.Kreusch, P.Kuhn, S.A.Lesley, M.D.Miller, K.Moy, E.Nigoghossian, J.Paulsen, K.Quijano, R.Reyes, C.Rife, G.Spraggon, R.C.Stevens, H.van den Bedem, J.Velasquez, J.Vincent, A.White, G.Wolf, Q.Xu, K.O.Hodgson, J.Wooley, I.A.Wilson.

ABSTRACT

No abstract given.

Selected figure(s)

Figure 1.
Figure 1. Crystal structure of Hsp33 from Thermotoga maritima. (A) Diagram showing the secondary structure elements in TM1394 (chain A) superimposed on its primary sequence. The -helices, 3[10]-helix, -bulges, and -turns are indicated. The -sheet strands are indicated by red letters (A, B, and C). -Hairpins are depicted as red loops, and cysteine residues coordinating the zinc are marked with blue dots. No electron density was found for residues 288-290 as indicated by purple dots. (B) Stereo ribbon diagram of TM1394 color-coded from N-terminus (blue) to C-terminus (red), showing the domain organization. Helices (H1-H10) and -strands ( 1- 13) are indicated.

Figure 2.
Figure 2. (A) TM1394 C-terminal zinc-finger domain in ribbon representation with zinc (pink sphere) and coordinating cysteine residues (Cys231, Cys233, Cys263, and Cys266) depicted in sticks. (B) Superposition of the TM1394 crystallographic dimer (gray) with the biological dimer of oxidized Hsp33 from E. coli (chain A, blue; chain B, orange) that contains the domain swap for residues 178-233. (C) Superposition of zinc sites in TM1394 and Hsp33 from Bacillus subtilis (gray with labels in brackets). Zn^2+ ions are shown as spheres, and the cysteines, as well as Tyr270(275) and Arg84(86) residues, are depicted in sticks.

The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2005, 61, 669-673) copyright 2005.