Structural Basis for Heme Recognition by HmuT Responsible for Heme Transport to the Heme Transporter in Corynebacterium glutamicum

Norifumi Muraki, Shigetoshi Aono

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)

Abstract

The crystal structure of HmuT from Corynebacterium glutamicum, which is a heme-binding protein in an ABC-type heme transporter system, HmuTUV, has been determined in the holo-form. Heme was accommodated with two different orientations in the central cleft, in which His141 and Tyr240 were coordinated to the heme as axial ligands.

Original languageEnglish
Pages (from-to)24-26
Number of pages3
JournalChemistry Letters
Volume45
Issue number1
DOIs
Publication statusPublished - 2016
Externally publishedYes

ASJC Scopus subject areas

  • Chemistry(all)

Fingerprint

Dive into the research topics of 'Structural Basis for Heme Recognition by HmuT Responsible for Heme Transport to the Heme Transporter in Corynebacterium glutamicum'. Together they form a unique fingerprint.

Cite this