3iha: Difference between revisions

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


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==Crystal Structure Analysis of Mglu in its glutamate form==
The line below this paragraph, containing "STRUCTURE_3iha", creates the "Structure Box" on the page.
<StructureSection load='3iha' size='340' side='right'caption='[[3iha]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3iha]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Micrococcus_luteus Micrococcus luteus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IHA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IHA 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]] 2.6&#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=GLU:GLUTAMIC+ACID'>GLU</scene></td></tr>
{{STRUCTURE_3iha|  PDB=3iha  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3iha FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3iha OCA], [https://pdbe.org/3iha PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3iha RCSB], [https://www.ebi.ac.uk/pdbsum/3iha PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3iha ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q4U1A6_MICLU Q4U1A6_MICLU]
== 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/ih/3iha_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=3iha ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glutaminase from Micrococcus luteus K-3 [Micrococcus glutaminase (Mglu); 456 amino acid residues (aa); 48 kDa] is a salt-tolerant enzyme. Our previous study determined the structure of its major 42-kDa fragment. Here, using new crystallization conditions, we determined the structures of the intact enzyme in the presence and absence of its product L-glutamate and its activator Tris, which activates the enzyme by sixfold. With the exception of a 'lid' part (26-29 aa) and a few other short stretches, the structures were all very similar over the entire polypeptide chain. However, the presence of the ligands significantly reduced the length of the disordered regions: 41 aa in the unliganded structure (N), 21 aa for L-glutamate (G), 8 aa for Tris (T) and 6 aa for both L-glutamate and Tris (TG). L-glutamate was identified in both the G and TG structures, whereas Tris was only identified in the TG structure. Comparison of the glutamate-binding site between Mglu and salt-labile glutaminase (YbgJ) from Bacillus subtilis showed significantly smaller structural changes of the protein part in Mglu. A comparison of the substrate-binding pocket of Mglu, which is highly specific for L-glutamine, with that of Erwinia carotovora asparaginase, which has substrates other than L-glutamine, shows that Mglu has a larger substrate-binding pocket that prevents the binding of L-asparagine with proper interactions.


===Crystal Structure Analysis of Mglu in its glutamate form===
Crystal structure of salt-tolerant glutaminase from Micrococcus luteus K-3 in the presence and absence of its product L-glutamate and its activator Tris.,Yoshimune K, Shirakihara Y, Wakayama M, Yumoto I FEBS J. 2010 Feb;277(3):738-48. Epub 2009 Dec 29. PMID:20050917<ref>PMID:20050917</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3iha" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_20050917}}, adds the Publication Abstract to the page
*[[Glutaminase 3D structures|Glutaminase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 20050917 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_20050917}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
3IHA is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Micrococcus_luteus Micrococcus luteus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IHA OCA].
 
==Reference==
<ref group="xtra">PMID:20050917</ref><references group="xtra"/>
[[Category: Glutaminase]]
[[Category: Micrococcus luteus]]
[[Category: Micrococcus luteus]]
[[Category: Shirakihara, Y.]]
[[Category: Shirakihara Y]]
[[Category: Yoshimune, K.]]
[[Category: Yoshimune K]]
[[Category: Hydrolase]]
[[Category: Salt-tolerant glutaminase]]
 
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Retrieved from "https://proteopedia.org/3iha"