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

Norifumi Muraki; Shigetoshi Aono

doi:10.1246/cl.150894

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 journal › Article › peer-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 language	English
Pages (from-to)	24-26
Number of pages	3
Journal	Chemistry Letters
Volume	45
Issue number	1
DOIs	https://doi.org/10.1246/cl.150894
Publication status	Published - 2016
Externally published	Yes

ASJC Scopus subject areas

Chemistry(all)

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10.1246/cl.150894

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title = "Structural Basis for Heme Recognition by HmuT Responsible for Heme Transport to the Heme Transporter in Corynebacterium glutamicum",

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.",

author = "Norifumi Muraki and Shigetoshi Aono",

note = "Publisher Copyright: {\textcopyright} 2016 The Chemical Society of Japan.",

year = "2016",

doi = "10.1246/cl.150894",

language = "English",

volume = "45",

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journal = "Chemistry Letters",

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AU - Muraki, Norifumi

AU - Aono, Shigetoshi

PY - 2016

Y1 - 2016

N2 - 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.

AB - 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.

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DO - 10.1246/cl.150894

M3 - Article

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JF - Chemistry Letters

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IS - 1

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

Abstract

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