6IEO

Crystal structure of Mycobacterium tuberculosis HtrA1 (Rv1223) in regulated conformation


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.83 Å
  • R-Value Free: 0.227 
  • R-Value Work: 0.191 

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Ligand Structure Quality Assessment 


This is version 1.1 of the entry. See complete history


Literature

The crystal structure of Mycobacterium tuberculosis high-temperature requirement A protein reveals an autoregulatory mechanism.

Gupta, A.K.Behera, D.Gopal, B.

(2018) Acta Crystallogr F Struct Biol Commun 74: 803-809

  • DOI: https://doi.org/10.1107/S2053230X18016217
  • Primary Citation of Related Structures:  
    6IEO

  • PubMed Abstract: 

    The crystal structure of Mycobacterium tuberculosis high-temperature requirement A (HtrA) protein was determined at 1.83 Å resolution. This membrane-associated protease is essential for the survival of M. tuberculosis. The crystal structure reveals that interactions between the PDZ domain and the catalytic domain in HtrA lead to an inactive conformation. This finding is consistent with its proposed role as a regulatory protease that is conditionally activated upon appropriate environmental triggers. The structure provides a basis for directed studies to evaluate the role of this essential protein and the regulatory pathways that are influenced by this protease.


  • Organizational Affiliation

    Molecular Biophysics Unit, Indian Institute of Science, C. V. Raman Road, Bangalore 560 012, India.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Probable serine protease HtrA (DEGP protein)314Mycobacterium tuberculosis H37RvMutation(s): 0 
Gene Names: htrARv1223
UniProt
Find proteins for O06291 (Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv))
Explore O06291 
Go to UniProtKB:  O06291
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO06291
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
PMS
Query on PMS

Download Ideal Coordinates CCD File 
B [auth A]phenylmethanesulfonic acid
C7 H8 O3 S
NIXKBAZVOQAHGC-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.83 Å
  • R-Value Free: 0.227 
  • R-Value Work: 0.191 
  • Space Group: H 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 107.114α = 90
b = 107.114β = 90
c = 61.529γ = 120
Software Package:
Software NamePurpose
REFMACrefinement
PDB_EXTRACTdata extraction
XDSdata reduction
Aimlessdata scaling
PHASERphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2018-12-19
    Type: Initial release
  • Version 1.1: 2023-11-22
    Changes: Data collection, Database references, Derived calculations, Refinement description