3ci4: Difference between revisions

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{{Seed}}
[[Image:3ci4.png|left|200px]]


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==Structure of the PduO-type ATP:co(I)rrinoid adenosyltransferase from Lactobacillus reuteri complexed with four-coordinate cob(II)inamide and ATP==
The line below this paragraph, containing "STRUCTURE_3ci4", creates the "Structure Box" on the page.
<StructureSection load='3ci4' size='340' side='right'caption='[[3ci4]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3ci4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Limosilactobacillus_reuteri Limosilactobacillus reuteri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CI4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CI4 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&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
{{STRUCTURE_3ci4|  PDB=3ci4  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ci4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ci4 OCA], [https://pdbe.org/3ci4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ci4 RCSB], [https://www.ebi.ac.uk/pdbsum/3ci4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ci4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q50EJ2_LIMRT Q50EJ2_LIMRT]
== 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/ci/3ci4_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3ci4 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
ATP:cob(I)alamin adenosyltransferases (ACAs) catalyze the transfer of the 5'-deoxyadenosyl moiety from ATP to the upper axial ligand position of cobalamin in the synthesis of coenzyme B 12. For the ACA-catalyzed reaction to proceed, cob(II)alamin must be reduced to cob(I)alamin in the enzyme active site. This reduction is facilitated through the generation of a four-coordinate cob(II)alamin intermediate on the enzyme. We have determined the high-resolution crystal structure of a human-type ACA from Lactobacillus reuteri with a four-coordinate cob(II)alamin bound in the enzyme active site and with the product, adenosylcobalamin, partially occupied in the active site. The assembled structures represent snapshots of the steps in the ACA-catalyzed formation of the cobalt-carbon bond of coenzyme B 12. The structures define the corrinoid binding site and provide visual evidence for a base-off, four-coordinate cob(II)alamin intermediate. The complete structural description of ACA-mediated catalysis reveals the molecular features of four-coordinate cob(II)alamin stabilization and provides additional insights into the molecular basis for dysfunction in human patients suffering from methylmalonic aciduria.


===Structure of the PduO-type ATP:co(I)rrinoid adenosyltransferase from Lactobacillus reuteri complexed with four-coordinate cob(II)inamide and ATP===
Structural characterization of a human-type corrinoid adenosyltransferase confirms that coenzyme B12 is synthesized through a four-coordinate intermediate.,St Maurice M, Mera P, Park K, Brunold TC, Escalante-Semerena JC, Rayment I Biochemistry. 2008 May 27;47(21):5755-66. Epub 2008 May 2. PMID:18452306<ref>PMID:18452306</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3ci4" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 18452306 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_18452306}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
3CI4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_reuteri Lactobacillus reuteri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CI4 OCA].
[[Category: Limosilactobacillus reuteri]]
 
[[Category: Escalante-Semerena JC]]
==Reference==
[[Category: Maurice MSt]]
Structural characterization of a human-type corrinoid adenosyltransferase confirms that coenzyme B12 is synthesized through a four-coordinate intermediate., St Maurice M, Mera P, Park K, Brunold TC, Escalante-Semerena JC, Rayment I, Biochemistry. 2008 May 27;47(21):5755-66. Epub 2008 May 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18452306 18452306]
[[Category: Mera PE]]
[[Category: Lactobacillus reuteri]]
[[Category: Rayment I]]
[[Category: Single protein]]
[[Category: Escalante-Semerena, J C.]]
[[Category: Maurice, M St.]]
[[Category: Mera, P E.]]
[[Category: Rayment, I.]]
[[Category: Adenosyltransferase variant]]
[[Category: Atp binding]]
[[Category: Corrin binding]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:08:54 2008''