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==Crystal Structure of the CBS domain pair of protein MJ0100 in complex with 5 -methylthioadenosine and S-adenosyl-L-methionine==
==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]] 1.79&Aring;' scene=''>
<StructureSection load='3kpc' size='340' side='right'caption='[[3kpc]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3kpc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. 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>
<table><tr><td colspan='2'>[[3kpc]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.79&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MTA:5-DEOXY-5-METHYLTHIOADENOSINE'>MTA</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></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 ATCC 43067])</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=3kpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kpc OCA], [https://pdbe.org/3kpc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kpc RCSB], [https://www.ebi.ac.uk/pdbsum/3kpc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kpc ProSAT]</span></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://pdbe.org/3kpc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kpc RCSB], [http://www.ebi.ac.uk/pdbsum/3kpc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3kpc ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ASST_METJA ASST_METJA] Required for O-acetylhomoserine sulfhydrylase (OAHS)-independent homocysteine (Hcy) biosynthesis. Together with MJ0099, catalyzes the condensation of sulfide with aspartate semialdehyde to generate homocysteine. Likely functions through persulfide intermediate.[UniProtKB:Q8TPT4]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=3kpc 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=3kpc ConSurf].
<div style="clear:both"></div>
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3kpc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 43067]]
[[Category: Large Structures]]
[[Category: Arribas, E A]]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Encinar, J A]]
[[Category: Arribas EA]]
[[Category: Fernandez, J A]]
[[Category: Encinar JA]]
[[Category: Garcia, I G]]
[[Category: Fernandez JA]]
[[Category: Kortazar, D]]
[[Category: Garcia IG]]
[[Category: Lucas, M]]
[[Category: Kortazar D]]
[[Category: Martinez-Chantar, M L]]
[[Category: Lucas M]]
[[Category: Martinez-Cruz, L A]]
[[Category: Martinez-Chantar ML]]
[[Category: Mato, J M]]
[[Category: Martinez-Cruz LA]]
[[Category: Oyenarte, I]]
[[Category: Mato JM]]
[[Category: Cbs domain]]
[[Category: Oyenarte I]]
[[Category: Conformational change]]
[[Category: S-adenosylmethionine]]
[[Category: Unknown function]]

Latest revision as of 13:17, 21 February 2024

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

3kpc is a 1 chain structure with sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.79Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ASST_METJA Required for O-acetylhomoserine sulfhydrylase (OAHS)-independent homocysteine (Hcy) biosynthesis. Together with MJ0099, catalyzes the condensation of sulfide with aspartate semialdehyde to generate homocysteine. Likely functions through persulfide intermediate.[UniProtKB:Q8TPT4]

Evolutionary Conservation

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

3kpc, resolution 1.79Å

Drag the structure with the mouse to rotate

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OCA
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