English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  The crystal structure of methenyltetrahydromethanopterin cyclohydrolase from the hyperthermophilic archaeon Methanopyrus kandleri

Grabarse, W., Vaupel, M., Vorholt, J. A., Shima, S., Thauer, R. K., Wittershagen, A., et al. (1999). The crystal structure of methenyltetrahydromethanopterin cyclohydrolase from the hyperthermophilic archaeon Methanopyrus kandleri. Structure, 7(10), 1257-1268. doi:10.1016/s0969-2126(00)80059-3.

Item is

Basic

show hide
Genre: Journal Article

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Grabarse, Wolfgang1, 2, Author           
Vaupel, Martin 2, Author
Vorholt, Julia A.2, Author
Shima, Seigo2, Author
Thauer, Rudolf K.2, Author
Wittershagen, Axel3, Author
Bourenkov, Gleb4, Author
Bartunik, Hans D.4, Author
Ermler, Ulrich1, Author           
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Max-Planck-Institut für terrestrische Mikrobiologie, 35043 Marburg, Germany, ou_persistent22              
3Institut für Anorganische Chemie, AK Prof. Kolbesen, 60439, Frankfurt, Germany, ou_persistent22              
4Max-Planck-Arbeitsgruppen für strukturelle Molekularbiologie, 22603, Hamburg, Germany, ou_persistent22              

Content

show
hide
Free keywords: halophilic enzyme; hyperthermophilicenzyme; methanogenic archaea; Methanopyruskandleri; methenyltetrahydromethanopterin; cyclohydrolase
 Abstract: BACKGROUND:The reduction of carbon dioxide to methane in methanogenic archaea involves the tetrahydrofolate analogue tetrahydromethanopterin (H4MPT) as a C1 unit carrier. In the third step of this reaction sequence, N5-formyl-H4MPT is converted to methenyl-H4MPT+ by the enzyme methenyltetrahydromethanopterin cyclohydrolase. The cyclohydrolase from the hyperthermophilic archaeon Methanopyrus kandleri (Mch) is extremely thermostable and adapted to a high intracellular concentration of lyotropic salts. RESULTS:Mch was crystallized and its structure solved at 2.0 A resolution using a combination of the single isomorphous replacement (SIR) and multiple anomalous dispersion (MAD) techniques. The structure of the homotrimeric enzyme reveals a new alpha/beta fold that is composed of two domains forming a large sequence-conserved pocket between them. Two phosphate ions were found in and adjacent to this pocket, respectively; the latter is displaced by the phosphate moiety of the substrate formyl-H4MPT according to a hypothetical model of the substrate binding. CONCLUSIONS:Although the exact position of the substrate is not yet known, the residues lining the active site of Mch could be tentatively assigned. Comparison of Mch with the tetrahydrofolate-specific cyclohydrolase/dehydrogenase reveals similarities in domain arrangement and in some active-site residues, whereas the fold appears to be different. The adaptation of Mch to high salt concentrations and high temperatures is reflected by the excess of acidic residues at the trimer surface and by the higher oligomerization state of Mch compared with its mesophtic counterparts.

Details

show
hide
Language(s): eng - English
 Dates: 1999-06-031999-03-301999-07-072000-03-201999-10-01
 Publication Status: Published in print
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/s0969-2126(00)80059-3
PMID: 10545331
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Structure
  Other : Structure
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: London : Cell Press
Pages: - Volume / Issue: 7 (10) Sequence Number: - Start / End Page: 1257 - 1268 Identifier: ISSN: 0969-2126
CoNE: https://pure.mpg.de/cone/journals/resource/954927002244_1