3pzt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:44, 21 February 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='3pzt' size='340' side='right'caption='[[3pzt]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
<StructureSection load='3pzt' size='340' side='right'caption='[[3pzt]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3pzt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PZT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PZT FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3pzt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PZT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PZT FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.97&#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;'>[[3pzu|3pzu]], [[3pzv|3pzv]]</div></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">eglS, bglC, gld, BSU18130 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr>
+
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </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=3pzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pzt OCA], [https://pdbe.org/3pzt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pzt RCSB], [https://www.ebi.ac.uk/pdbsum/3pzt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pzt 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=3pzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pzt OCA], [https://pdbe.org/3pzt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pzt RCSB], [https://www.ebi.ac.uk/pdbsum/3pzt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pzt ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/GUN2_BACSU GUN2_BACSU]
-
Cellulases participate in a number of biological events such as plant cell wall remodeling, nematode parasitism and microbial carbon uptake. Their ability to depolymerize crystalline cellulose is of great biotechnological interest for environmentally-compatible production of fuels from lignocellulosic biomass. However, industrial use of cellulases is somewhat limited both by their low catalytic efficiency and stability. In this work, we conducted a detailed functional and structural characterization of the thermostable cellulase 5A from Bacillus subtilis (BsCel5A), which consists of a GH5 catalytic domain fused to a family 3 carbohydrate-binding module (CBM3). NMR structural analysis revealed that the Bacillus CBM3 represents a new subfamily, which lacks the classical calcium-binding motif and variations in NMR frequencies in the presence of cellopentaose showed the importance of polar residues in the carbohydrate interaction. Together with the catalytic domain, the CBM3 forms a large planar surface for cellulose recognition, which conducts the substrate in a proper conformation to the active site and increases enzymatic efficiency. Notably, the manganese ion demonstrated to have a hyper-stabilizing effect on BsCel5A and by using deletion constructs and X-ray crystallography, we determined that this effect maps to a negatively charged motif located at the opposite face of the catalytic site.
+
-
 
+
-
Dissecting structure-function-stability relationships of a thermostable GH5-CBM3 cellulase from Bacillus subtilis 168.,Santos C, Paiva J, Sforca M, Neves J, Navarro R, Cota J, Akao P, Hoffmam ZB, Meza A, Smetana J, Nogueira M, Polikarpov I, Xavier-Neto J, Squina F, Ward RJ, Ruller R, Zeri A, Murakami MT Biochem J. 2011 Sep 1. PMID:21880019<ref>PMID:21880019</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 3pzt" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==
*[[Glucanase 3D structures|Glucanase 3D structures]]
*[[Glucanase 3D structures|Glucanase 3D structures]]
-
== References ==
 
-
<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Bacsu]]
+
[[Category: Bacillus subtilis subsp. subtilis str. 168]]
-
[[Category: Cellulase]]
+
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Akao, P K]]
+
[[Category: Akao PK]]
-
[[Category: Meza, A N]]
+
[[Category: Meza AN]]
-
[[Category: Murakami, M T]]
+
[[Category: Murakami MT]]
-
[[Category: Paiva, J H]]
+
[[Category: Paiva JH]]
-
[[Category: Ruller, R]]
+
[[Category: Ruller R]]
-
[[Category: Santos, C R]]
+
[[Category: Santos CR]]
-
[[Category: Silva, J C]]
+
[[Category: Silva JC]]
-
[[Category: Squina, F M]]
+
[[Category: Squina FM]]
-
[[Category: Ward, R J]]
+
[[Category: Ward RJ]]
-
[[Category: Alpha/beta barrel]]
+
-
[[Category: Cellulose binding]]
+
-
[[Category: Glycosyl hydrolase]]
+
-
[[Category: Hydrolase]]
+

Current revision

Structure of the endo-1,4-beta-glucanase from Bacillus subtilis 168 with manganese(II) ion

PDB ID 3pzt

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3pzt"
Personal tools