3kpc: Difference between revisions
m Protected "3kpc" [edit=sysop:move=sysop] |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal Structure of the CBS domain pair of protein MJ0100 in complex with 5 -methylthioadenosine and S-adenosyl-L-methionine== | |||
<StructureSection load='3kpc' size='340' side='right' caption='[[3kpc]], [[Resolution|resolution]] 1.79Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3kpc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KPC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KPC FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MTA:5-DEOXY-5-METHYLTHIOADENOSINE'>MTA</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3kpb|3kpb]], [[3kpd|3kpd]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MJ0100 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 Methanocaldococcus jannaschii])</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=3kpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kpc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3kpc RCSB], [http://www.ebi.ac.uk/pdbsum/3kpc PDBsum]</span></td></tr> | |||
</table> | |||
== 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/kp/3kpc_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/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Cystathionine beta-synthase (CBS) domains are small motifs that are present in proteins with completely different functions. Several genetic diseases in humans have been associated with mutations in their sequence, which has made them promising targets for rational drug design. The protein MJ0100 from Methanocaldococcus jannaschii includes a DUF39 domain of so far unknown function and a CBS domain pair (Bateman domain) at its C-terminus. This work presents the crystallographic analysis of four different states of the CBS motif pair of MJ0100 in complex with different numbers of S-adenosyl-L-methionine (SAM) and S-methyl-5'-thioadenosine (MTA) ligands, providing evidence that ligand-induced conformational reorganization of Bateman domain dimers could be an important regulatory mechanism. These observations are in contrast to what is known from most of the other Bateman domain structures but are supported by recent studies on the magnesium transporter MgtE. Our structures represent the first example of a CBS domain protein complexed with SAM and/or MTA and might provide a structural basis for understanding the molecular mechanisms regulated by SAM upon binding to the C-terminal domain of human CBS, whose structure remains unknown. | |||
Binding of S-methyl-5'-thioadenosine and S-adenosyl-L-methionine to protein MJ0100 triggers an open-to-closed conformational change in its CBS motif pair.,Lucas M, Encinar JA, Arribas EA, Oyenarte I, Garcia IG, Kortazar D, Fernandez JA, Mato JM, Martinez-Chantar ML, Martinez-Cruz LA J Mol Biol. 2010 Feb 26;396(3):800-20. Epub 2009 Dec 21. PMID:20026078<ref>PMID:20026078</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Methanocaldococcus jannaschii]] | [[Category: Methanocaldococcus jannaschii]] | ||
[[Category: Arribas, E A | [[Category: Arribas, E A]] | ||
[[Category: Encinar, J A | [[Category: Encinar, J A]] | ||
[[Category: Fernandez, J A | [[Category: Fernandez, J A]] | ||
[[Category: Garcia, I G | [[Category: Garcia, I G]] | ||
[[Category: Kortazar, D | [[Category: Kortazar, D]] | ||
[[Category: Lucas, M | [[Category: Lucas, M]] | ||
[[Category: Martinez-Chantar, M L | [[Category: Martinez-Chantar, M L]] | ||
[[Category: Martinez-Cruz, L A | [[Category: Martinez-Cruz, L A]] | ||
[[Category: Mato, J M | [[Category: Mato, J M]] | ||
[[Category: Oyenarte, I | [[Category: Oyenarte, I]] | ||
[[Category: Cbs domain]] | [[Category: Cbs domain]] | ||
[[Category: Conformational change]] | [[Category: Conformational change]] | ||
[[Category: S-adenosylmethionine]] | [[Category: S-adenosylmethionine]] | ||
[[Category: Unknown function]] | [[Category: Unknown function]] | ||
Revision as of 20:57, 18 December 2014
Crystal Structure of the CBS domain pair of protein MJ0100 in complex with 5 -methylthioadenosine and S-adenosyl-L-methionineCrystal Structure of the CBS domain pair of protein MJ0100 in complex with 5 -methylthioadenosine and S-adenosyl-L-methionine
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCystathionine beta-synthase (CBS) domains are small motifs that are present in proteins with completely different functions. Several genetic diseases in humans have been associated with mutations in their sequence, which has made them promising targets for rational drug design. The protein MJ0100 from Methanocaldococcus jannaschii includes a DUF39 domain of so far unknown function and a CBS domain pair (Bateman domain) at its C-terminus. This work presents the crystallographic analysis of four different states of the CBS motif pair of MJ0100 in complex with different numbers of S-adenosyl-L-methionine (SAM) and S-methyl-5'-thioadenosine (MTA) ligands, providing evidence that ligand-induced conformational reorganization of Bateman domain dimers could be an important regulatory mechanism. These observations are in contrast to what is known from most of the other Bateman domain structures but are supported by recent studies on the magnesium transporter MgtE. Our structures represent the first example of a CBS domain protein complexed with SAM and/or MTA and might provide a structural basis for understanding the molecular mechanisms regulated by SAM upon binding to the C-terminal domain of human CBS, whose structure remains unknown. Binding of S-methyl-5'-thioadenosine and S-adenosyl-L-methionine to protein MJ0100 triggers an open-to-closed conformational change in its CBS motif pair.,Lucas M, Encinar JA, Arribas EA, Oyenarte I, Garcia IG, Kortazar D, Fernandez JA, Mato JM, Martinez-Chantar ML, Martinez-Cruz LA J Mol Biol. 2010 Feb 26;396(3):800-20. Epub 2009 Dec 21. PMID:20026078[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||||