1y5y

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[[Image:1y5y.gif|left|200px]]
[[Image:1y5y.gif|left|200px]]
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{{Structure
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|PDB= 1y5y |SIZE=350|CAPTION= <scene name='initialview01'>1y5y</scene>, resolution 2.00&Aring;
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The line below this paragraph, containing "STRUCTURE_1y5y", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|GENE= fae ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=500 Thermomicrobium roseum])
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{{STRUCTURE_1y5y| PDB=1y5y | SCENE= }}
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|RELATEDENTRY=[[1y60|1Y60]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y5y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y5y OCA], [http://www.ebi.ac.uk/pdbsum/1y5y PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1y5y RCSB]</span>
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'''Structure of the tetrahydromethanopterin dependent formaldehyde-activating enzyme (Fae) from Methylobacterium extorquens AM1'''
'''Structure of the tetrahydromethanopterin dependent formaldehyde-activating enzyme (Fae) from Methylobacterium extorquens AM1'''
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[[Category: Thauer, R K.]]
[[Category: Thauer, R K.]]
[[Category: Vorholt, J A.]]
[[Category: Vorholt, J A.]]
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[[Category: beta-alpha-beta left handed crossover]]
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[[Category: Beta-alpha-beta left handed crossover]]
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[[Category: flexible c-terminus]]
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[[Category: Flexible c-terminus]]
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[[Category: pentamer]]
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[[Category: Pentamer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:54:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:59:13 2008''
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Revision as of 12:54, 3 May 2008

Template:STRUCTURE 1y5y

Structure of the tetrahydromethanopterin dependent formaldehyde-activating enzyme (Fae) from Methylobacterium extorquens AM1


Overview

Tetrahydromethanopterin (H4 MPT) is a tetrahydrofolate analogue involved as a C1 carrier in the metabolism of various groups of microorganisms. How H4MPT is bound to the respective C1 unit converting enzymes remained elusive. We describe here the structure of the homopentameric formaldehyde-activating enzyme (Fae) from Methylobacterium extorquens AM1 established at 2.0 angstrom without and at 1.9 angstrom with methylene-H4MPT bound. Methylene-H4MPT is bound in an "S"-shaped conformation into the cleft formed between two adjacent subunits. Coenzyme binding is accompanied by side chain rearrangements up to 5 angstrom and leads to a rigidification of the C-terminal arm, a formation of a new hydrophobic cluster, and an inversion of the amide side chain of Gln88. Methylene-H4MPT in Fae shows a characteristic kink between the tetrahydropyrazine and the imidazolidine rings of 70 degrees that is more pronounced than that reported for free methylene-H4MPT in solution (50 degrees). Fae is an essential enzyme for energy metabolism and formaldehyde detoxification of this bacterium and catalyzes the formation of methylene-H4MPT from H4MPT and formaldehyde. The molecular mechanism ofthis reaction involving His22 as acid catalyst is discussed.

About this Structure

1Y5Y is a Single protein structure of sequence from Thermomicrobium roseum. Full crystallographic information is available from OCA.

Reference

How an enzyme binds the C1 carrier tetrahydromethanopterin. Structure of the tetrahydromethanopterin-dependent formaldehyde-activating enzyme (Fae) from Methylobacterium extorquens AM1., Acharya P, Goenrich M, Hagemeier CH, Demmer U, Vorholt JA, Thauer RK, Ermler U, J Biol Chem. 2005 Apr 8;280(14):13712-9. Epub 2005 Jan 4. PMID:15632161 Page seeded by OCA on Sat May 3 15:54:47 2008

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