1z69
From Proteopedia
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|PDB= 1z69 |SIZE=350|CAPTION= <scene name='initialview01'>1z69</scene>, resolution 2.61Å | |PDB= 1z69 |SIZE=350|CAPTION= <scene name='initialview01'>1z69</scene>, resolution 2.61Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=1PG:2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL'>1PG</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=F42:COENZYME+F420'>F42</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/5,10-methylenetetrahydromethanopterin_reductase 5,10-methylenetetrahydromethanopterin reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.99.11 1.5.99.11] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/5,10-methylenetetrahydromethanopterin_reductase 5,10-methylenetetrahydromethanopterin reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.99.11 1.5.99.11] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ezw|1EZW]], [[1f07|1F07]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1z69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z69 OCA], [http://www.ebi.ac.uk/pdbsum/1z69 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1z69 RCSB]</span> | ||
}} | }} | ||
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[[Category: Thauer, R K.]] | [[Category: Thauer, R K.]] | ||
[[Category: Warkentin, E.]] | [[Category: Warkentin, E.]] | ||
| - | [[Category: 1PG]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: F42]] | ||
[[Category: (alpha]] | [[Category: (alpha]] | ||
[[Category: beta)8 barrel]] | [[Category: beta)8 barrel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:29:43 2008'' |
Revision as of 22:29, 30 March 2008
| |||||||
| , resolution 2.61Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | 5,10-methylenetetrahydromethanopterin reductase, with EC number 1.5.99.11 | ||||||
| Related: | 1EZW, 1F07
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of methylenetetrahydromethanopterin reductase (Mer) in complex with coenzyme F420
Overview
Methylenetetratetrahydromethanopterin reductase (Mer) is involved in CO(2) reduction to methane in methanogenic archaea and catalyses the reversible reduction of methylenetetrahydromethanopterin (methylene-H(4)MPT) to methyl-H(4)MPT with coenzyme F(420)H(2), which is a reduced 5'-deazaflavin. Mer was recently established as a TIM barrel structure containing a nonprolyl cis-peptide bond but the binding site of the substrates remained elusive. We report here on the crystal structure of Mer in complex with F(420) at 2.6 A resolution. The isoalloxazine ring is present in a pronounced butterfly conformation, being induced from the Re-face of F(420) by a bulge that contains the non-prolyl cis-peptide bond. The bindingmode of F(420) is very similar to that in F(420)-dependent alcohol dehydrogenase Adf despite the low sequence identity of 21%. Moreover, binding of F(420) to the apoenzyme was only associated with minor conformational changes of the polypeptide chain. These findings allowed us to build an improved model of FMN into its binding site in bacterial luciferase, which belongs to the same structural family as Mer and Adf and also contains a nonprolyl cis-peptide bond in an equivalent position.
About this Structure
1Z69 is a Single protein structure of sequence from Methanosarcina barkeri. Full crystallographic information is available from OCA.
Reference
Crystal structure of methylenetetrahydromethanopterin reductase (Mer) in complex with coenzyme F420: Architecture of the F420/FMN binding site of enzymes within the nonprolyl cis-peptide containing bacterial luciferase family., Aufhammer SW, Warkentin E, Ermler U, Hagemeier CH, Thauer RK, Shima S, Protein Sci. 2005 Jul;14(7):1840-9. Epub 2005 Jun 3. PMID:15937276
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