3u95: Difference between revisions

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<StructureSection load='3u95' size='340' side='right'caption='[[3u95]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3u95' size='340' side='right'caption='[[3u95]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3u95]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thenn Thenn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U95 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U95 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3u95]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_neapolitana_DSM_4359 Thermotoga neapolitana DSM 4359]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U95 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U95 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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]] 1.998&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1obb|1obb]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTN_1830 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=309803 THENN])</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=3u95 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u95 OCA], [https://pdbe.org/3u95 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u95 RCSB], [https://www.ebi.ac.uk/pdbsum/3u95 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u95 ProSAT]</span></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=3u95 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u95 OCA], [https://pdbe.org/3u95 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u95 RCSB], [https://www.ebi.ac.uk/pdbsum/3u95 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u95 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/B9KAM3_THENN B9KAM3_THENN]
Glycoside hydrolase family 4 (GH4) represents an unusual group of glucosidases with a requirement for NAD(+), Mn(2+), and reducing conditions. We found a putative alpha-glucosidase belonging to GH4 in hyperthermophilic Gram-negative bacterium Thermotoga neapolitana. In this study, we recombinantly expressed the putative alpha-glycosidase from T. neapolitana, and determined the crystal structure of the protein at a resolution of 2.0A in the presence of Mn(2+) but in the absence of NAD(+). The structure showed the dimeric assembly and the Mn(2+) coordination that other GH4 enzymes share. In comparison, we observed structural changes in T. neapolitana alpha-glucosidase by the binding of NAD(+), which also increased the thermostability. Numerous arginine-mediated salt-bridges were observed in the structure, and we confirmed that the salt bridges correlated with the thermostability of the proteins. Disruption of the salt bridge that linked N-terminal and C-terminal parts at the surface dramatically decreased the thermostability. A mutation that changed the internal salt bridge to a hydrogen bond also decreased the thermostability of the protein. This study will help us to understand the function of the putative glucosidase and the structural features that affect the thermostability of the protein.
 
Crystal structure and thermostability of a putative alpha-glucosidase from Thermotoga neapolitana.,Yun BY, Jun SY, Kim NA, Yoon BY, Piao S, Park SH, Jeong SH, Lee H, Ha NC Biochem Biophys Res Commun. 2011 Dec 9;416(1-2):92-8. Epub 2011 Nov 10. PMID:22093829<ref>PMID:22093829</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3u95" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Thenn]]
[[Category: Thermotoga neapolitana DSM 4359]]
[[Category: Ha, N C]]
[[Category: Ha NC]]
[[Category: Jun, S Y]]
[[Category: Jun SY]]
[[Category: Piao, S]]
[[Category: Piao S]]
[[Category: Yoon, B Y]]
[[Category: Yoon BY]]
[[Category: Yun, B Y]]
[[Category: Yun BY]]
[[Category: Cytosol]]
[[Category: Hydrolase]]
[[Category: Hydrolysis]]

Latest revision as of 08:38, 20 March 2024

Crystal structure of a putative alpha-glucosidase from Thermotoga neapolitana

3u95, resolution 2.00Å

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