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<StructureSection load='4fio' size='340' side='right'caption='[[4fio]], [[Resolution|resolution]] 1.37&Aring;' scene=''>
<StructureSection load='4fio' size='340' side='right'caption='[[4fio]], [[Resolution|resolution]] 1.37&Aring;' 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 [https://en.wikipedia.org/wiki/Methanobrevibacter_ruminantium_M1 Methanobrevibacter ruminantium M1]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4FIO FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EEE:ETHYL+ACETATE'>EEE</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.37&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qlm|1qlm]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EEE:ETHYL+ACETATE'>EEE</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mch, mru_1619 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=634498 METRM])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4fio FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fio OCA], [https://pdbe.org/4fio PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fio RCSB], [https://www.ebi.ac.uk/pdbsum/4fio PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fio ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methenyltetrahydromethanopterin_cyclohydrolase Methenyltetrahydromethanopterin cyclohydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.27 3.5.4.27] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fio FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fio OCA], [http://pdbe.org/4fio PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fio RCSB], [http://www.ebi.ac.uk/pdbsum/4fio PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fio ProSAT]</span></td></tr>
</table>
</table>
== 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]  
[https://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&reg;/PubMed&reg;, 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 3D structures|Cyclohydrolase 3D structures]]
*[[Cyclohydrolase 3D structures|Cyclohydrolase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Methenyltetrahydromethanopterin cyclohydrolase]]
[[Category: Methanobrevibacter ruminantium M1]]
[[Category: Metrm]]
[[Category: Beattie AK]]
[[Category: Beattie, A K]]
[[Category: Carbone V]]
[[Category: Carbone, V]]
[[Category: Ronimus RS]]
[[Category: Ronimus, R S]]
[[Category: Schofield LR]]
[[Category: Schofield, L R]]
[[Category: Sutherland-Smith AJ]]
[[Category: Sutherland-Smith, A J]]
[[Category: Hydrolase]]
[[Category: Hydrolysis]]
[[Category: Methanogenesis]]
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