1gc2: Difference between revisions

New page: left|200px<br /><applet load="1gc2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gc2, resolution 2.00Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1gc2.jpg|left|200px]]<br /><applet load="1gc2" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1gc2, resolution 2.00&Aring;" />
'''CRYSTAL STRUCTURE OF THE PYRIDOXAL-5'-PHOSPHATE DEPENDENT L-METHIONINE GAMMA-LYASE FROM PSEUDOMONAS PUTIDA'''<br />


==Overview==
==CRYSTAL STRUCTURE OF THE PYRIDOXAL-5'-PHOSPHATE DEPENDENT L-METHIONINE GAMMA-LYASE FROM PSEUDOMONAS PUTIDA==
L-Methionine gamma-lyase (MGL) catalyzes the pyridoxal 5'-phosphate (PLP), dependent alpha,gamma-elimination of L-methionine. We have determined two, crystal structures of MGL from Pseudomonas putida using MAD, (multiwavelength anomalous diffraction) and molecular replacement methods., The structures have been refined to an R-factor of 21.1% at 2.0 and 1.7 A, resolution using synchrotron radiation diffraction data. A homotetramer, with 222 symmetry is built up by non-crystallographic symmetry. Two, monomers associate to build the active dimer. The spatial fold of, subunits, with three functionally distinct domains and their quarternary, arrangement, is similar to those of L-cystathionine beta-lyase and, L-cystathionine gamma-synthase from Escherichia coli.
<StructureSection load='1gc2' size='340' side='right'caption='[[1gc2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1gc2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GC2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GC2 FirstGlance]. <br>
</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></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=1gc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gc2 OCA], [https://pdbe.org/1gc2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gc2 RCSB], [https://www.ebi.ac.uk/pdbsum/1gc2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gc2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MEGL_PSEPU MEGL_PSEPU]
== 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/gc/1gc2_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/main_output.php?pdb_ID=1gc2 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
L-Methionine gamma-lyase (MGL) catalyzes the pyridoxal 5'-phosphate (PLP) dependent alpha,gamma-elimination of L-methionine. We have determined two crystal structures of MGL from Pseudomonas putida using MAD (multiwavelength anomalous diffraction) and molecular replacement methods. The structures have been refined to an R-factor of 21.1% at 2.0 and 1.7 A resolution using synchrotron radiation diffraction data. A homotetramer with 222 symmetry is built up by non-crystallographic symmetry. Two monomers associate to build the active dimer. The spatial fold of subunits, with three functionally distinct domains and their quarternary arrangement, is similar to those of L-cystathionine beta-lyase and L-cystathionine gamma-synthase from Escherichia coli.


==About this Structure==
Crystal structure of the pyridoxal 5'-phosphate dependent L-methionine gamma-lyase from Pseudomonas putida.,Motoshima H, Inagaki K, Kumasaka T, Furuichi M, Inoue H, Tamura T, Esaki N, Soda K, Tanaka N, Yamamoto M, Tanaka H J Biochem. 2000 Sep;128(3):349-54. PMID:10965031<ref>PMID:10965031</ref>
1GC2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Active as [http://en.wikipedia.org/wiki/Methionine_gamma-lyase Methionine gamma-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.11 4.4.1.11] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GC2 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structure of the pyridoxal 5'-phosphate dependent L-methionine gamma-lyase from Pseudomonas putida., Motoshima H, Inagaki K, Kumasaka T, Furuichi M, Inoue H, Tamura T, Esaki N, Soda K, Tanaka N, Yamamoto M, Tanaka H, J Biochem (Tokyo). 2000 Sep;128(3):349-54. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10965031 10965031]
</div>
[[Category: Methionine gamma-lyase]]
<div class="pdbe-citations 1gc2" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Methionine gamma-lyase 3D structures|Methionine gamma-lyase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas putida]]
[[Category: Pseudomonas putida]]
[[Category: Single protein]]
[[Category: Esaki N]]
[[Category: Esaki, N.]]
[[Category: Furuichi M]]
[[Category: Furuichi, M.]]
[[Category: Inagaki K]]
[[Category: Inagaki, K.]]
[[Category: Inoue H]]
[[Category: Inoue, H.]]
[[Category: Kumasaka T]]
[[Category: Kumasaka, T.]]
[[Category: Motoshima H]]
[[Category: Motoshima, H.]]
[[Category: Soda K]]
[[Category: Soda, K.]]
[[Category: Tamura T]]
[[Category: Tamura, T.]]
[[Category: Tanaka H]]
[[Category: Tanaka, H.]]
[[Category: Tanaka N]]
[[Category: Tanaka, N.]]
[[Category: Yamamoto M]]
[[Category: Yamamoto, M.]]
[[Category: pyridoxal-5'-phosphate]]
 
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