PDBsum entry 6cdb

Transcription

PDB id: 6cdb

Contents

Protein chains

97 a.a.

Ligands

PG4

Metals

_NA

_CL ×4

_ZN ×2

Waters ×78

PDB id:

6cdb

Name:

Transcription

Title:

Crystal structure of v66l czra in the zn(ii)bound state

Structure:

Arsr family transcriptional regulator. Chain: a, b. Synonym: czra protein,hth-type transcriptional repressor czra, putative hth-type transcriptional repressor czra,repressor protein, transcriptional regulator,zn(ii) or co(ii)-specific transcriptional repressor protein. Engineered: yes

Source:

Staphylococcus aureus. Organism_taxid: 1280. Gene: rzca, czra, czra, afo97_05125, b9z04_11610, b9z08_13310, bji53_13345, bn1321_350009, ep54_06885, eq90_13065, ers072738_01903, ers072840_01825, hmpref3211_00009. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.99Å R-factor: 0.197 R-free: 0.228

Authors:

D.A.Capdevila,G.Campanello,G.Gonzalez-Gutierrez,D.P.Giedroc

Key ref:

D.A.Capdevila et al. (2018). Functional Role of Solvent Entropy and Conformational Entropy of Metal Binding in a Dynamically Driven Allosteric System. J Am Chem Soc, 140, 9108-9119. PubMed id: 29953213 DOI: 10.1021/jacs.8b02129

Date:

08-Feb-18 Release date: 11-Jul-18

Protein chains

O85142  (O85142_STAAU) -  ArsR family transcriptional regulator from Staphylococcus aureus

Seq: 106 a.a.

Struc: 97 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1021/jacs.8b02129

J Am Chem Soc 140:9108-9119 (2018)

PubMed id: 29953213

Functional Role of Solvent Entropy and Conformational Entropy of Metal Binding in a Dynamically Driven Allosteric System.

D.A.Capdevila, K.A.Edmonds, G.C.Campanello, H.Wu, G.Gonzalez-Gutierrez, D.P.Giedroc.

ABSTRACT

Allostery is a regulatory phenomenon whereby ligand binding to one site influences the binding of the same or a different ligand to another site on a macromolecule. The physical origins of allosteric regulation remain under intense investigation. In general terms, ligand-induced structural changes, perturbations of residue-specific dynamics, and surrounding solvent molecules all potentially contribute to the global energetics of allostery. While the role of solvent is generally well understood in regulatory events associated with major protein structural rearrangements, the degree to which protein dynamics impact solvent degrees of freedom is unclear, particularly in cases of dynamically driven allostery. With the aid of new crystal structures, extensive calorimetric and residue-specific dynamics studies over a range of time scales and temperatures, we dissect for the first time the relative degree to which changes in solvent entropy and residue-specific dynamics impact dynamically driven, allosteric inhibition of DNA binding by Zn in the zinc efflux repressor, CzrA (chromosomal zinc-regulated repressor). We show that non-native residue-specific dynamics in allosterically impaired CzrA mutants are accompanied by significant perturbations in solvent entropy that cannot be predicted from crystal structures. We conclude that functional dynamics are not necessarily restricted to protein residues but involve surface water molecules that may be responding to ligand (Zn)-mediated perturbations in protein internal motions that define the conformational ensemble, rather than major structural rearrangements.