1q7m: Difference between revisions

← Older edit Newer edit →

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

OCA

@@ Line 3: / Line 3: @@
 <StructureSection load='1q7m' size='340' side='right'caption='[[1q7m]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1q7m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q7M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q7M FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1q7m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q7M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q7M FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1q7q|1q7q]], [[1q7z|1q7z]], [[1q85|1q85]], [[1q8a|1q8a]]</div></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]] 2.1&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Methionine_synthase Methionine synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.13 2.1.1.13] </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=1q7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q7m OCA], [https://pdbe.org/1q7m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q7m RCSB], [https://www.ebi.ac.uk/pdbsum/1q7m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q7m ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q9WYA5_THEMA Q9WYA5_THEMA]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 18: / Line 19: @@
 </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=1q7m ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-B(12)-dependent methionine synthase (MetH) is a large modular enzyme that utilizes the cobalamin cofactor as a methyl donor or acceptor in three separate reactions. Each methyl transfer occurs at a different substrate-binding domain and requires a different arrangement of modules. In the catalytic cycle, the cobalamin-binding domain carries methylcobalamin to the homocysteine (Hcy) domain to form methionine and returns cob(I)alamin to the folate (Fol) domain for remethylation by methyltetrahydrofolate (CH(3)-H(4)folate). Here, we describe crystal structures of a fragment of MetH from Thermotoga maritima comprising the domains that bind Hcy and CH(3)-H(4)folate. These substrate-binding domains are (beta alpha)(8) barrels packed tightly against one another with their barrel axes perpendicular. The properties of the domain interface suggest that the two barrels remain associated during catalysis. The Hcy and CH(3)-H(4)folate substrates are bound at the C termini of their respective barrels in orientations that position them for reaction with cobalamin, but the two active sites are separated by approximately 50 A. To complete the catalytic cycle, the cobalamin-binding domain must travel back and forth between these distant active sites.
-Structures of the N-terminal modules imply large domain motions during catalysis by methionine synthase.,Evans JC, Huddler DP, Hilgers MT, Romanchuk G, Matthews RG, Ludwig ML Proc Natl Acad Sci U S A. 2004 Mar 16;101(11):3729-36. Epub 2004 Jan 29. PMID:14752199<ref>PMID:14752199</ref>
+==See Also==
+*[[Methionine synthase 3D structures|Methionine synthase 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1q7m" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 43589]]
 [[Category: Large Structures]]
-[[Category: Methionine synthase]]
+[[Category: Thermotoga maritima]]
-[[Category: Evans, J C]]
+[[Category: Evans JC]]
-[[Category: Hilgers, M T]]
+[[Category: Hilgers MT]]
-[[Category: Huddler, D P]]
+[[Category: Huddler DP]]
-[[Category: Ludwig, M L]]
+[[Category: Ludwig ML]]
-[[Category: Matthews, R G]]
+[[Category: Matthews RG]]
-[[Category: Romanchuk, G]]
+[[Category: Romanchuk G]]
-[[Category: Cobalamin]]
-[[Category: Folate]]
-[[Category: Homocysteine]]
-[[Category: Methionine]]
-[[Category: Transferase]]
-[[Category: Vitamin b12]]