1b5t: Difference between revisions

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-[[Image:1b5t.gif|left|200px]]
-<!--
+==ESCHERICHIA COLI METHYLENETETRAHYDROFOLATE REDUCTASE==
-The line below this paragraph, containing "STRUCTURE_1b5t", creates the "Structure Box" on the page.
+<StructureSection load='1b5t' size='340' side='right'caption='[[1b5t]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1b5t]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B5T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B5T FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr>
-{{STRUCTURE_1b5t|  PDB=1b5t  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1b5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b5t OCA], [https://pdbe.org/1b5t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b5t RCSB], [https://www.ebi.ac.uk/pdbsum/1b5t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b5t ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/METF_ECOLI METF_ECOLI] Methylenetetrahydrofolate reductase required to generate the methyl groups necessary for methionine synthetase to convert homocysteine to methionine.<ref>PMID:14275142</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b5/1b5t_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1b5t ConSurf].
+<div style="clear:both"></div>
-'''ESCHERICHIA COLI METHYLENETETRAHYDROFOLATE REDUCTASE'''
+==See Also==
+*[[Methylenetetrahydrofolate reductase 3D structures|Methylenetetrahydrofolate reductase 3D structures]]
+== References ==
-==Overview==
+<references/>
-Elevated plasma homocysteine levels are associated with increased risk for cardiovascular disease and neural tube defects in humans. Folate treatment decreases homocysteine levels and dramatically reduces the incidence of neural tube defects. The flavoprotein methylenetetrahydrofolate reductase (MTHFR) is a likely target for these actions of folate. The most common genetic cause of mildly elevated plasma homocysteine in humans is the MTHFR polymorphism A222V (base change C677--&gt;T). The X-ray analysis of E. coli MTHFR, reported here, provides a model for the catalytic domain that is shared by all MTHFRs. This domain is a beta8alpha8 barrel that binds FAD in a novel fashion. Ala 177, corresponding to Ala 222 in human MTHFR, is near the bottom of the barrel and distant from the FAD. The mutation A177V does not affect Km or k(cat) but instead increases the propensity for bacterial MTHFR to lose its essential flavin cofactor. Folate derivatives protect wild-type and mutant E. coli enzymes against flavin loss, and protect human MTHFR and the A222V mutant against thermal inactivation, suggesting a mechanism by which folate treatment reduces homocysteine levels.
+__TOC__
+</StructureSection>
-==About this Structure==
-B5T is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B5T OCA].
-==Reference==
-The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia., Guenther BD, Sheppard CA, Tran P, Rozen R, Matthews RG, Ludwig ML, Nat Struct Biol. 1999 Apr;6(4):359-65. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10201405 10201405]
-[[Category: Deleted entry]]
 [[Category: Escherichia coli]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Guenther, B D.]]
+[[Category: Guenther BD]]
-[[Category: Ludwig, M L.]]
+[[Category: Ludwig ML]]
-[[Category: Matthews, R G.]]
+[[Category: Matthews RG]]
-[[Category: Rozen, R.]]
+[[Category: Rozen R]]
-[[Category: Sheppard, C A.]]
+[[Category: Sheppard CA]]
-[[Category: Tran, P.]]
+[[Category: Tran P]]
-[[Category: Beta alpha barrel]]
-[[Category: Reductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:06:24 2008''