4qce: Difference between revisions

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 ==Crystal structure of recombinant alkali thermostable GH10 xylanase from Bacillus sp. NG-27==
-<StructureSection load='4qce' size='340' side='right' caption='[[4qce]], [[Resolution|resolution]] 2.32&Aring;' scene=''>
+<StructureSection load='4qce' size='340' side='right'caption='[[4qce]], [[Resolution|resolution]] 2.32&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4qce]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QCE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QCE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4qce]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._NG-27 Bacillus sp. NG-27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QCE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QCE FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2.32&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2f8q|2f8q]], [[2fgl|2fgl]], [[4qcf|4qcf]], [[4qdm|4qdm]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] </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=4qce FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qce OCA], [https://pdbe.org/4qce PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qce RCSB], [https://www.ebi.ac.uk/pdbsum/4qce PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qce 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=4qce FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qce OCA], [http://pdbe.org/4qce PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qce RCSB], [http://www.ebi.ac.uk/pdbsum/4qce PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qce ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/O30700_9BACI O30700_9BACI]
-Although several factors have been suggested to contribute to thermostability, the stabilization strategies used by proteins are still enigmatic. Studies on a recombinant xylanase from Bacilllus sp. NG-27 (RBSX), which has the ubiquitous (beta/alpha)8 -triosephosphate isomerase barrel fold, showed that just a single mutation, V1L, although not located in any secondary structural element, markedly enhanced the stability from 70 degrees C to 75 degrees C without loss of catalytic activity. Conversely, the V1A mutation at the same position decreased the stability of the enzyme from 70 degrees C to 68 degrees C. To gain structural insights into how a single extreme N-terminus mutation can markedly influence the thermostability of the enzyme, we determined the crystal structure of RBSX and the two mutants. On the basis of computational analysis of their crystal structures, including residue interaction networks, we established a link between N-terminal to C-terminal contacts and RBSX thermostability. Our study reveals that augmenting N-terminal to C-terminal noncovalent interactions is associated with enhancement of the stability of the enzyme. In addition, we discuss several lines of evidence supporting a connection between N-terminal to C-terminal noncovalent interactions and protein stability in different proteins. We propose that the strategy of mutations at the termini could be exploited with a view to modulate stability without compromising enzymatic activity, or in general, protein function in diverse folds where N and C termini are in close proximity. DATABASE: The coordinates of RBSX, V1A and V1L have been deposited in the PDB database under the accession numbers 4QCE, 4QCF, and 4QDM, respectively.
-Structural insights into N-terminal to C-terminal interactions and implications for thermostability of a (beta/alpha)8-triosephosphate isomerase barrel enzyme.,Mahanta P, Bhardwaj A, Kumar K, Reddy VS, Ramakumar S FEBS J. 2015 Sep;282(18):3543-55. doi: 10.1111/febs.13355. Epub 2015 Jul 15. PMID:26102498<ref>PMID:26102498</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4qce" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Endo-1,4-beta-xylanase]]
+[[Category: Bacillus sp. NG-27]]
-[[Category: Bhardwaj, A]]
+[[Category: Large Structures]]
-[[Category: Mahanta, P]]
+[[Category: Bhardwaj A]]
-[[Category: Ramakumar, S]]
+[[Category: Mahanta P]]
-[[Category: Reddy, V S]]
+[[Category: Ramakumar S]]
-[[Category: Gh10 xylanase]]
+[[Category: Reddy VS]]
-[[Category: Glycosyl hydrolase]]
-[[Category: Hydrolase]]