1qlm: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,329,557 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,329,557 edits
No edit summary
Line 1: Line 1:
[[Image:1qlm.jpg|left|200px]]
{{Seed}}
[[Image:1qlm.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1qlm|  PDB=1qlm  |  SCENE=  }}  
{{STRUCTURE_1qlm|  PDB=1qlm  |  SCENE=  }}  


'''THE CRYSTAL STRUCTURE OF METHENYLTETRAHYDROMETHANOPTERIN CYCLOHYDROLASE FROM THE HYPERTHERMOPHILIC ARCHAEON METHANOPYRUS KANDLERI'''
===THE CRYSTAL STRUCTURE OF METHENYLTETRAHYDROMETHANOPTERIN CYCLOHYDROLASE FROM THE HYPERTHERMOPHILIC ARCHAEON METHANOPYRUS KANDLERI===




==Overview==
<!--
BACKGROUND: The reduction of carbon dioxide to methane in methanogenic archaea involves the tetrahydrofolate analogue tetrahydromethanopterin (H(4)MPT) as a C(1) unit carrier. In the third step of this reaction sequence, N(5)-formyl-H(4)MPT is converted to methenyl-H(4)MPT(+) 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-H(4)MPT 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.
The line below this paragraph, {{ABSTRACT_PUBMED_10545331}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 10545331 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_10545331}}


==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Biological methanogenesis]]
[[Category: Biological methanogenesis]]
[[Category: Tetrahydromethanopterin]]
[[Category: Tetrahydromethanopterin]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:25:17 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:02:00 2008''

Revision as of 07:02, 29 July 2008

File:1qlm.png

Template:STRUCTURE 1qlm

THE CRYSTAL STRUCTURE OF METHENYLTETRAHYDROMETHANOPTERIN CYCLOHYDROLASE FROM THE HYPERTHERMOPHILIC ARCHAEON METHANOPYRUS KANDLERI

Template:ABSTRACT PUBMED 10545331

About this Structure

1QLM is a Single protein structure of sequence from Methanopyrus kandleri. Full crystallographic information is available from OCA.

Reference

The crystal structure of methenyltetrahydromethanopterin cyclohydrolase from the hyperthermophilic archaeon Methanopyrus kandleri., Grabarse W, Vaupel M, Vorholt JA, Shima S, Thauer RK, Wittershagen A, Bourenkov G, Bartunik HD, Ermler U, Structure. 1999 Oct 15;7(10):1257-68. PMID:10545331

Page seeded by OCA on Tue Jul 29 10:02:00 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1qlm&oldid=737635"