PDBsum entry 6hcd

Nuclear protein

PDB id: 6hcd

Contents

Protein chains

133 a.a.

135 a.a.

Ligands

UNL ×4

ACT ×2

Metals

_CL ×9

Waters ×221

PDB id:

6hcd

Name:

Nuclear protein

Title:

Structure of universal stress protein from archaeoglobus fulgidus

Structure:

Universal stress protein. Chain: a, b, c, d. Engineered: yes

Source:

Archaeoglobus fulgidus. Organism_taxid: 2234. Gene: af_0826. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: codonplus ril.

Resolution:

1.90Å R-factor: 0.169 R-free: 0.207

Authors:

I.A.Shumilin,J.I.Loch,M.Cymborowski,X.Xu,A.Edwards,R.Di Leo, I.G.Shabalin,A.Joachimiak,A.Savchenko,W.Minor,Midwest Center For Structural Genomics (Mcsg)

Key ref:

K.L.Tkaczuk et al. (2013). Structural and functional insight into the universal stress protein family. Evol Appl, 6, 434-449. PubMed id: 23745136 DOI: 10.1111/eva.12057

Date:

14-Aug-18 Release date: 29-Aug-18

Supersedes:

3dlo

Protein chains

O29432  (O29432_ARCFU) -  UspA domain-containing protein from Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)

Seq: 134 a.a.

Struc: 133 a.a.

Protein chain

O29432  (O29432_ARCFU) -  UspA domain-containing protein from Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)

Seq: 134 a.a.

Struc: 135 a.a.

DOI no: 10.1111/eva.12057

Evol Appl 6:434-449 (2013)

PubMed id: 23745136

Structural and functional insight into the universal stress protein family.

K.L.Tkaczuk, I.A Shumilin, M.Chruszcz, E.Evdokimova, A.Savchenko, W.Minor.

ABSTRACT

We present the crystal structures of two universal stress proteins (USP) from Archaeoglobus fulgidus and Nitrosomonas europaea in both apo- and ligand-bound forms. This work is the first complete synthesis of the structural properties of 26 USP available in the Protein Data Bank, over 75% of which were determined by structure genomics centers with no additional information provided. The results of bioinformatic analyses of all available USP structures and their sequence homologs revealed that these two new USP structures share overall structural similarity with structures of USPs previously determined. Clustering and cladogram analyses, however, show how they diverge from other members of the USP superfamily and show greater similarity to USPs from organisms inhabiting extreme environments. We compared them with other archaeal and bacterial USPs and discuss their similarities and differences in context of structure, sequential motifs, and potential function. We also attempted to group all analyzed USPs into families, so that assignment of the potential function to those with no experimental data available would be possible by extrapolation.