6joy: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
 
Line 3: Line 3:
<StructureSection load='6joy' size='340' side='right'caption='[[6joy]], [[Resolution|resolution]] 2.39&Aring;' scene=''>
<StructureSection load='6joy' size='340' side='right'caption='[[6joy]], [[Resolution|resolution]] 2.39&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6joy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43812 Atcc 43812]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JOY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JOY FirstGlance]. <br>
<table><tr><td colspan='2'>[[6joy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodothermus_marinus Rhodothermus marinus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JOY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JOY FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">glgB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29549 ATCC 43812])</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]] 2.392&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/1,4-alpha-glucan_branching_enzyme 1,4-alpha-glucan branching enzyme], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.18 2.4.1.18] </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=6joy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6joy OCA], [https://pdbe.org/6joy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6joy RCSB], [https://www.ebi.ac.uk/pdbsum/6joy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6joy 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=6joy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6joy OCA], [https://pdbe.org/6joy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6joy RCSB], [https://www.ebi.ac.uk/pdbsum/6joy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6joy ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/GLGB_RHOMR GLGB_RHOMR]] Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.  
[https://www.uniprot.org/uniprot/GLGB_RHOMR GLGB_RHOMR] Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A gene encoding 1,4-alpha-glucan branching enzyme (GBE, EC 2.4.1.18) from the extremely thermophilic bacterium Rhodothermus obamensis STB05 was successfully cloned and expressed in Escherichia coli. Extracellular expression of the recombinant enzyme (R.o-GBE) was achieved with a yield of 1080mg/L. Then it was purified and further characterized biochemically. R.o-GBE was optimally active at pH 7.0 and 65 degrees C. It remained stable at temperatures up to 80 degrees C and had a half-life at 85 degrees C of approximately 31min. Far-UV circular dichroism and intrinsic fluorescence analyses revealed that high temperatures reduced its activity by changing the secondary and tertiary structure of R.o-GBE. The enzyme had broad pH stability between pH 3.0 and 11.0at 4 degrees C, and preferred weakly acidic conditions at high temperatures. None of the metal ions enhanced the activity of R.o-GBE, but Ca(2+) may be required for its activity. Its specific activity with amylopectin was 6651 U/mg, which is much higher than that reported for other GBEs. Its excellent thermostability, broad pH stability, and high specific activity make R.o-GBE highly suitable for industrial applications.
 
Expression and characterization of an extremely thermophilic 1,4-alpha-glucan branching enzyme from Rhodothermus obamensis STB05.,Wang Z, Xin C, Li C, Gu Z, Cheng L, Hong Y, Ban X, Li Z Protein Expr Purif. 2019 Dec;164:105478. doi: 10.1016/j.pep.2019.105478. Epub, 2019 Aug 14. PMID:31421223<ref>PMID:31421223</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6joy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: 1,4-alpha-glucan branching enzyme]]
[[Category: Atcc 43812]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ban, X F]]
[[Category: Rhodothermus marinus]]
[[Category: Gu, Z B]]
[[Category: Ban XF]]
[[Category: Jiang, H M]]
[[Category: Gu ZB]]
[[Category: Jin, T C]]
[[Category: Jiang HM]]
[[Category: Li, C M]]
[[Category: Jin TC]]
[[Category: Li, Z F]]
[[Category: Li CM]]
[[Category: Wang, Z]]
[[Category: Li ZF]]
[[Category: Branching enzyme]]
[[Category: Wang Z]]
[[Category: Carbohydrate]]
Retrieved from "https://proteopedia.org/6joy"