4fio: Difference between revisions
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==Crystal Structure of Methenyltetrahydromethanopterin Cyclohydrolase from Methanobrevibacter ruminantium== | ==Crystal Structure of Methenyltetrahydromethanopterin Cyclohydrolase from Methanobrevibacter ruminantium== | ||
<StructureSection load='4fio' size='340' side='right' caption='[[4fio]], [[Resolution|resolution]] 1.37Å' scene=''> | <StructureSection load='4fio' size='340' side='right'caption='[[4fio]], [[Resolution|resolution]] 1.37Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4fio]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Metrm Metrm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FIO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FIO FirstGlance]. <br> | <table><tr><td colspan='2'>[[4fio]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Metrm Metrm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FIO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FIO FirstGlance]. <br> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/D3E4S5_METRM D3E4S5_METRM]] Catalyzes the reversible interconversion of 5-formyl-H(4)MPT to methenyl-H(4)MPT(+) (By similarity).[HAMAP-Rule:MF_00486] | [[http://www.uniprot.org/uniprot/D3E4S5_METRM D3E4S5_METRM]] Catalyzes the reversible interconversion of 5-formyl-H(4)MPT to methenyl-H(4)MPT(+) (By similarity).[HAMAP-Rule:MF_00486] | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Methenyltetrahydromethanopterin cyclohydrolase (Mch) is involved in the methanogenesis pathway of archaea as a C1 unit carrier where N(5) -formyl-tetrahydromethanopterin is converted to methenyl-tetrahydromethanopterin. Mch from Methanobrevibacter ruminantium was cloned, purified, crystallized and its crystal structure solved at 1.37 A resolution. A biologically active trimer, the enzyme is composed of two domains including an N-terminal domain of six alpha-helices encompassing a series of four beta-sheets and a predominantly anti-parallel beta-sheet at the C-terminus flanked on one side by alpha-helices. Sequence and structural alignments have helped identify residues involved in substrate binding and trimer formation. | |||
The crystal structure of methenyltetrahydromethanopterin cyclohydrolase from Methanobrevibacter ruminantium.,Carbone V, Schofield LR, Beattie AK, Sutherland-Smith AJ, Ronimus RS Proteins. 2013 Nov;81(11):2064-70. doi: 10.1002/prot.24372. Epub 2013 Aug 23. PMID:23873651<ref>PMID:23873651</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4fio" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Cyclohydrolase|Cyclohydrolase]] | *[[Cyclohydrolase 3D structures|Cyclohydrolase 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Methenyltetrahydromethanopterin cyclohydrolase]] | [[Category: Methenyltetrahydromethanopterin cyclohydrolase]] | ||
[[Category: Metrm]] | [[Category: Metrm]] | ||
Revision as of 06:13, 3 July 2019
Crystal Structure of Methenyltetrahydromethanopterin Cyclohydrolase from Methanobrevibacter ruminantium
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