6JSB

Crystal structure of Heme binding protein HtaB from Corynebacterium glutamicum

PDB DOI: https://doi.org/10.2210/pdb6JSB/pdb

Classification: HEME-BINDING PROTEIN
Organism(s): Corynebacterium glutamicum ATCC 13032
Expression System: Escherichia coli BL21(DE3)
Mutation(s): No

Deposited: 2019-04-08 Released: 2019-11-20
Deposition Author(s): Muraki, N., Aono, S.
Funding Organization(s): Japan Society for the Promotion of Science

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.70 Å
R-Value Free: 0.198
R-Value Work: 0.177
R-Value Observed: 0.178

wwPDB Validation 3D Report Full Report

Ligand Structure Quality Assessment

This is version 1.2 of the entry. See complete history.

Literature

Structural basis for the heme transfer reaction in heme uptake machinery from Corynebacteria.

Muraki, N., Kitatsuji, C., Okamoto, Y., Uchida, T., Ishimori, K., Aono, S.

(2019) Chem Commun (Camb) 55: 13864-13867

PubMed: 31670736 Search on PubMed
DOI: https://doi.org/10.1039/c9cc07369h
Primary Citation of Related Structures:
6JS9, 6JSA, 6JSB, 6JSC, 6JSD

PubMed Abstract:
The crystal structures of the conserved region domains of HtaA and HtaB, which act as heme binding/transport proteins in the heme uptake machinery in Corynebacterium glutamicum, are determined for the first time. The molecular mechanism of heme transfer among these proteins is proposed based on the spectroscopic and structural analyses.

Organizational Affiliation

Department of Creative Research, Exploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji-cho, Okazaki 444-8787, Japan. aono@ims.ac.jp.

Macromolecule Content

Total Structure Weight: 45.67 kDa
Atom Count: 3,631
Modelled Residue Count: 397
Deposited Residue Count: 406
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Hypothetical membrane protein	A, B	203	Corynebacterium glutamicum ATCC 13032	Mutation(s): 0 Gene Names: Cgl0392
UniProt
Find proteins for Q8NTB5 (Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025)) Explore Q8NTB5 Go to UniProtKB: Q8NTB5
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q8NTB5
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 2 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
HEM Query on HEM Download Ideal Coordinates CCD File SDF format, chain C [auth A] SDF format, chain F [auth B] MOL2 format, chain C [auth A] MOL2 format, chain F [auth B]	C [auth A], F [auth B]	PROTOPORPHYRIN IX CONTAINING FE C₃₄ H₃₂ Fe N₄ O₄ KABFMIBPWCXCRK-RGGAHWMASA-L		Interactions Focus chain C [auth A] Focus chain F [auth B] Interactions & Density Focus chain C [auth A] Focus chain F [auth B]
CA Query on CA Download Ideal Coordinates CCD File SDF format, chain D [auth A] SDF format, chain E [auth A] MOL2 format, chain D [auth A] MOL2 format, chain E [auth A]	D [auth A], E [auth A]	CALCIUM ION Ca BHPQYMZQTOCNFJ-UHFFFAOYSA-N		Interactions Focus chain D [auth A] Focus chain E [auth A] Interactions & Density Focus chain D [auth A] Focus chain E [auth A]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.70 Å
R-Value Free: 0.198
R-Value Work: 0.177
R-Value Observed: 0.178
Space Group: C 1 2 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 235.17	α = 90
b = 33.73	β = 121.14
c = 126.62	γ = 90

Software Package:

Software Name	Purpose
PHENIX	refinement
XDS	data reduction
XSCALE	data scaling
PHASER	phasing

Structure Validation

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Ligand Structure Quality Assessment

Entry History & Funding Information

Deposition Data

Released Date: 2019-11-20

Deposition Author(s):

Muraki, N.

Aono, S.

Funding Organization	Location	Grant Number
Japan Society for the Promotion of Science	Japan	17K15081

Revision History (Full details and data files)

Version 1.0: 2019-11-20
Type: Initial release
Version 1.1: 2019-11-27
Changes: Database references
Version 1.2: 2023-11-22
Changes: Data collection, Database references, Derived calculations, Refinement description