His84 rather than His35 is the active site histidine in the corrinoid protein MtrA of the energy conserving methyltransferase complex from Methanobacterium thermoautotrophicum

被引：12

作者：

Sauer, K ^{[1
]}

Thauer, RK ^{[1
]}

机构：

[1] Univ Marburg, Fachbereich Biol, Max Planck Inst Terr Mikrobiol, D-35043 Marburg, Germany

来源：

FEBS LETTERS | 1998年 / 436卷 / 03期

关键词：

corrinoid protein; B-12 binding motif; N-5-methyltetrahydromethanopterin : coenzyme M methyltransferase; methanogenic archaeon;

D O I：

10.1016/S0014-5793(98)01180-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The energy conserving corrinoid containing MtrA-H complex from Methanobacterium thermoautotrophicum is composed of eight different subunits of which MtrA harbors the corrinoid prosthetic group, the corrinoid being bound in the base-off/His-on configuration. Based on sequence comparisons it was recently proposed that His(35) Of MtrA is the active site histidine, We report here that His(84) rather than His(35) is the axial ligand to the cobamide in MtrA, (C) 1998 Federation of European Biochemical Societies.

引用

页码：401 / 402

页数：2

共 15 条

[1] Clustered genes encoding the methyltransferases of methanogenesis from monomethylamine
Burke, SA
Lo, SL
Krzycki, JA
[J]. JOURNAL OF BACTERIOLOGY, 1998, 180 (13) : 3432 - 3440
[2] Pathways of energy conservation in methanogenic archaea
Deppenmeier, U
Muller, V
Gottschalk, G
[J]. ARCHIVES OF MICROBIOLOGY, 1996, 165 (03) : 149 - 163
[3] HOW A PROTEIN BINDS B-12 - A 3.0-ANGSTROM X-RAY STRUCTURE OF B-12-BINDING DOMAINS OF METHIONINE SYNTHASE
DRENNAN, CL
HUANG, S
DRUMMOND, JT
MATTHEWS, RG
LUDWIG, ML
[J]. SCIENCE, 1994, 266 (5191) : 1669 - 1674
[4] THE ENERGY CONSERVING N-5-METHYLTETRAHYDROMETHANOPTERIN-COENZYME-M METHYLTRANSFERASE COMPLEX FROM METHANOBACTERIUM-THERMOAUTOTROPHICUM IS COMPOSED OF 8 DIFFERENT SUBUNITS
HARMS, U
WEISS, DS
GARTNER, P
LINDER, D
THAUER, RK
[J]. EUROPEAN JOURNAL OF BIOCHEMISTRY, 1995, 228 (03): : 640 - 648
[5] The corrinoid-containing 23-kDa subunit MtrA of the energy-conserving N-5-methyltetrahydromethanopterin:coenzyme M methyltransferase complex from Methanobacterium thermoautotrophicum - EPR spectroscopic evidence for a histidine residue as a cobalt ligand of the cobamide
Harms, U
Tauer, RK
[J]. EUROPEAN JOURNAL OF BIOCHEMISTRY, 1996, 241 (01): : 149 - 154
[6] HARMS U, 1998, VITAMIN B12 B12 PROT, P157
[7] Cloning, sequencing and expression of the genes encoding the sodium translocating N5-methyltetrahydromethanopterin:coenzyme M methyltransferase of the methylotrophic archaeon Methanosarcina mazei Go1
Lienard, T
Gottschalk, G
[J]. FEBS LETTERS, 1998, 425 (02) : 204 - 208
[8] Structure-based perspectives on B-12-dependent enzymes
Ludwig, ML
Matthews, RG
[J]. ANNUAL REVIEW OF BIOCHEMISTRY, 1997, 66 : 269 - 313
[9] CLONING AND SEQUENCING OF GLUTAMATE MUTASE COMPONENT-S FROM CLOSTRIDIUM-TETANOMORPHUM - HOMOLOGIES WITH OTHER COBALAMIN-DEPENDENT ENZYMES
MARSH, ENG
HOLLOWAY, DE
[J]. FEBS LETTERS, 1992, 310 (02) : 167 - 170
[10] COENZYME B-12 IS COORDINATED BY HISTIDINE AND NOT DIMETHYLBENZIMIDAZOLE ON METHYLMALONYL-COA MUTASE
PADMAKUMAR, R
TAOKA, S
PADMAKUMAR, R
BANERJEE, R
[J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1995, 117 (26) : 7033 - 7034

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