4fio
From Proteopedia
(Difference between revisions)
| Line 4: | Line 4: | ||
== Structural highlights == | == Structural highlights == | ||
<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> | <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" id="ligandDat"><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]] 1.37Å</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='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='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> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[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] | [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®/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 3D structures|Cyclohydrolase 3D structures]] | *[[Cyclohydrolase 3D structures|Cyclohydrolase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal Structure of Methenyltetrahydromethanopterin Cyclohydrolase from Methanobrevibacter ruminantium
| |||||||||||
