3mmu: Difference between revisions

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{{Seed}}
[[Image:3mmu.jpg|left|200px]]


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==Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima==
The line below this paragraph, containing "STRUCTURE_3mmu", creates the "Structure Box" on the page.
<StructureSection load='3mmu' size='340' side='right'caption='[[3mmu]], [[Resolution|resolution]] 2.20&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'>[[3mmu]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MMU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MMU 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]] 2.201&#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=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
{{STRUCTURE_3mmu|  PDB=3mmu  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3mmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mmu OCA], [https://pdbe.org/3mmu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mmu RCSB], [https://www.ebi.ac.uk/pdbsum/3mmu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mmu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9X273_THEMA Q9X273_THEMA]
== 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/mm/3mmu_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=3mmu ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Tm_Cel5A, which belongs to family 5 of the glycoside hydrolases, is an extremely stable enzyme among the endo-acting glycosidases present in the hyperthermophilic organism Thermotoga maritima. Members of GH5 family shows a common (beta/alpha)(8) TIM-barrel fold in which the catalytic acid/base and nucleophile are located on strands beta-4 and beta-7 of the barrel fold. Thermally resistant cellulases are desirable for lignocellulosic biofuels production and the Tm_Cel5A is an excellent candidate for use in the degradation of polysaccharides present on biomass. This paper describes two Tm_Cel5A structures (crystal forms I and II) solved at 2.20 and 1.85A resolution, respectively. Our analyses of the Tm_Cel5A structure and comparison to a mesophilic GH5 provides a basis for the thermostability associated with Tm_Cel5A. Furthermore, both crystal forms of Tm_Cel5A possess a cadmium (Cd(2+)) ion bound between the two catalytic residues. Activity assays of Tm_Cel5A confirmed a strong inhibition effect in the presence of Cd(2+) metal ions demonstrating competition with the natural substrate for the active site. Based on the structural information we have obtained for Tm_Cel5A, protein bioengineering can be used to potentially increase the thermostability of mesophilic cellulase enzymes.


===Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima===
Biochemical characterization and crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima.,Pereira JH, Chen Z, McAndrew RP, Sapra R, Chhabra SR, Sale KL, Simmons BA, Adams PD J Struct Biol. 2010 Jul 3. PMID:20599513<ref>PMID:20599513</ref>


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


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_20599513}}, adds the Publication Abstract to the page
*[[Glucanase 3D structures|Glucanase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 20599513 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_20599513}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
3MMU is a 8 chains structure with sequences from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MMU OCA].
 
==Reference==
<ref group="xtra">PMID:20599513</ref><references group="xtra"/>
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: Adams, P D.]]
[[Category: Adams PD]]
[[Category: Chen, Z.]]
[[Category: Chen Z]]
[[Category: Chhabra, S R.]]
[[Category: Chhabra SR]]
[[Category: McAndrew, R P.]]
[[Category: McAndrew RP]]
[[Category: Pereira, J H.]]
[[Category: Pereira JH]]
[[Category: Sale, K L.]]
[[Category: Sale KL]]
[[Category: Sapra, R.]]
[[Category: Sapra R]]
[[Category: Simmons, B A.]]
[[Category: Simmons BA]]
[[Category: Hydrolase]]
[[Category: Tim-barrel fold]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 28 12:39:19 2010''
Retrieved from "https://proteopedia.org/3mmu"