3apt: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:3apt.jpg|left|200px]]
-<!--
+==properties and crystal structure of methylenetetrahydrofolate reductase from Thermus thermophilus HB8==
-The line below this paragraph, containing "STRUCTURE_3apt", creates the "Structure Box" on the page.
+<StructureSection load='3apt' size='340' side='right'caption='[[3apt]], [[Resolution|resolution]] 1.85&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'>[[3apt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3APT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3APT 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]] 1.85&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
-{{STRUCTURE_3apt|  PDB=3apt  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3apt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3apt OCA], [https://pdbe.org/3apt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3apt RCSB], [https://www.ebi.ac.uk/pdbsum/3apt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3apt ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q5SLG6_THET8 Q5SLG6_THET8]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+BACKGROUND: Methylenetetrahydrofolate reductase (MTHFR) is one of the enzymes involved in homocysteine metabolism. Despite considerable genetic and clinical attention, the reaction mechanism and regulation of this enzyme are not fully understood because of difficult production and poor stability. While recombinant enzymes from thermophilic organisms are often stable and easy to prepare, properties of thermostable MTHFRs have not yet been reported. METHODOLOGY/PRINCIPAL FINDINGS: MTHFR from Thermus thermophilus HB8, a homologue of Escherichia coli MetF, has been expressed in E. coli and purified. The purified MTHFR was chiefly obtained as a heterodimer of apo- and holo-subunits, that is, one flavin adenine dinucleotide (FAD) prosthetic group bound per dimer. The crystal structure of the holo-subunit was quite similar to the beta(8)alpha(8) barrel of E. coli MTHFR, while that of the apo-subunit was a previously unobserved closed form. In addition, the intersubunit interface of the dimer in the crystals was different from any of the subunit interfaces of the tetramer of E. coli MTHFR. Free FAD could be incorporated into the apo-subunit of the purified Thermus enzyme after purification, forming a homodimer of holo-subunits. Comparison of the crystal structures of the heterodimer and the homodimer revealed different intersubunit interfaces, indicating a large conformational change upon FAD binding. Most of the biochemical properties of the heterodimer and the homodimer were the same, except that the homodimer showed approximately 50% activity per FAD-bound subunit in folate-dependent reactions. CONCLUSIONS/SIGNIFICANCE: The different intersubunit interfaces and rearrangement of subunits of Thermus MTHFR may be related to human enzyme properties, such as the allosteric regulation by S-adenosylmethionine and the enhanced instability of the Ala222Val mutant upon loss of FAD. Whereas E. coli MTHFR was the only structural model for human MTHFR to date, our findings suggest that Thermus MTHFR will be another useful model for this important enzyme.
-===properties and crystal structure of methylenetetrahydrofolate reductase from Thermus thermophilus HB8===
+Properties and Crystal Structure of Methylenetetrahydrofolate Reductase from Thermus thermophilus HB8.,Igari S, Ohtaki A, Yamanaka Y, Sato Y, Yohda M, Odaka M, Noguchi K, Yamada K PLoS One. 2011;6(8):e23716. Epub 2011 Aug 15. PMID:21858212<ref>PMID:21858212</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3apt" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_21858212}}, adds the Publication Abstract to the page
+*[[Methylenetetrahydrofolate reductase 3D structures|Methylenetetrahydrofolate reductase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 21858212 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_21858212}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-[[3apt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3APT OCA].
+[[Category: Thermus thermophilus HB8]]
+[[Category: Yamada K]]
-==Reference==
-<ref group="xtra">PMID:021858212</ref><references group="xtra"/>
-[[Category: Thermus thermophilus]]
-[[Category: Yamada, K.]]
-[[Category: Flavin]]
-[[Category: Oxidoreductase]]
-[[Category: Tim barrel]]