3o7w: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
Line 1: Line 1:


==The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1==
==The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1==
<StructureSection load='3o7w' size='340' side='right' caption='[[3o7w]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3o7w' size='340' side='right'caption='[[3o7w]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3o7w]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3mnt 3mnt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O7W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O7W FirstGlance]. <br>
<table><tr><td colspan='2'>[[3o7w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3mnt 3mnt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O7W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O7W FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></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&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LCMT1, LCMT, CGI-68 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3o7w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o7w OCA], [http://pdbe.org/3o7w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3o7w RCSB], [http://www.ebi.ac.uk/pdbsum/3o7w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3o7w ProSAT]</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=3o7w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o7w OCA], [https://pdbe.org/3o7w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o7w RCSB], [https://www.ebi.ac.uk/pdbsum/3o7w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o7w ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/LCMT1_HUMAN LCMT1_HUMAN]] Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.<ref>PMID:10600115</ref>
[https://www.uniprot.org/uniprot/LCMT1_HUMAN LCMT1_HUMAN] Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.<ref>PMID:10600115</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 20: Line 20:
</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=3o7w ConSurf].
</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=3o7w ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Leucine carboxyl methyltransferase 1 (LCMT1) methylates the terminal carboxyl group of the leucine 309 residue of human protein phosphatase 2A (PP2A). PP2A, a key regulator of many cellular processes, has recently generated additional interest as a potential cancer-therapeutic target. The status of PP2A methylation impacts upon the selection of the regulatory subunit by the PP2A core enzyme, thus directing its activity and subcellular localization. An X-ray crystal structure of human LCMT1 protein in complex with the cofactor S-adenosylmethionine (AdoMet) has been solved to a resolution of 2 A. The structure enables the postulation of a mode of interaction with protein phosphatase PP2A and provides a platform for further functional studies of the regulation of methylation of PP2A.
The structure of human leucine carboxyl methyltransferase 1 that regulates protein phosphatase PP2A.,Tsai ML, Cronin N, Djordjevic S Acta Crystallogr D Biol Crystallogr. 2011 Jan;67(Pt 1):14-24. Epub 2010, Dec 16. PMID:21206058<ref>PMID:21206058</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3o7w" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Cronin, N]]
[[Category: Large Structures]]
[[Category: Djordjevic, S]]
[[Category: Cronin N]]
[[Category: Tsai, M L]]
[[Category: Djordjevic S]]
[[Category: Modified rossmann fold]]
[[Category: Tsai ML]]
[[Category: Pp2a]]
[[Category: Transferase]]

Latest revision as of 11:32, 20 March 2024

The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1

Structural highlights

3o7w is a 1 chain structure with sequence from Homo sapiens. This structure supersedes the now removed PDB entry 3mnt. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LCMT1_HUMAN Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ De Baere I, Derua R, Janssens V, Van Hoof C, Waelkens E, Merlevede W, Goris J. Purification of porcine brain protein phosphatase 2A leucine carboxyl methyltransferase and cloning of the human homologue. Biochemistry. 1999 Dec 14;38(50):16539-47. PMID:10600115

3o7w, resolution 2.00Å

Drag the structure with the mouse to rotate

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

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=3o7w&oldid=4103996"