5m99: Difference between revisions

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~~'''Unreleased structure'''~~

The ~~entry 5m99~~ is ~~ON HOLD~~

==Functional Characterization and Crystal Structure of Thermostable Amylase from Thermotoga petrophila, reveals High Thermostability and an Archaic form of Dimerization==

== Structural highlights ==

<table><tr><td colspan='2'>[[5m99]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_petrophila_RKU-1 Thermotoga petrophila RKU-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M99 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5M99 FirstGlance]. <br>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.96Å</td></tr>

<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></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=5m99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m99 OCA], [https://pdbe.org/5m99 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5m99 RCSB], [https://www.ebi.ac.uk/pdbsum/5m99 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5m99 ProSAT]</span></td></tr>

</table>

== Function ==

[https://www.uniprot.org/uniprot/A0A059TXD8_THEP1 A0A059TXD8_THEP1]

== Publication Abstract from PubMed ==

Thermostable alpha-amylases have many industrial applications and are therefore continuously explored from novel sources. We present the characterization of a novel putative alpha-amylase gene product (Tp-AmyS) cloned from Thermotoga petrophila. The purified recombinant enzyme is highly thermostable and able to hydrolyze starch into dextrin between 90 and 100 degrees C, with optimum activity at 98 degrees C and pH8.5. The activity increased in the presence of Rb1+, K1+ and Ca2+ ions, whereas other ions inhibited activity. The crystal structure of Tp-AmyS at 1.7A resolution showed common features of the GH-13 family, however was apparently found to be a dimer. Several residues from one monomer interacted with a docked acarbose, an inhibitor of Tp-AmyS, in the other monomer, suggesting catalytic cooperativity within the dimer. The most striking feature of the dimer was that it resembled the dimerization of salivary amylase from a previous crystal structure, and thus could be a functional feature of some amylases.

~~Authors~~:

Functional characterization and crystal structure of thermostable amylase from Thermotoga petrophila, reveals high thermostability and an unusual form of dimerization.,Hameed U, Price I, Ikram-Ul-Haq, Ke A, Wilson DB, Mirza O Biochim Biophys Acta. 2017 Jun 22;1865(10):1237-1245. doi:, 10.1016/j.bbapap.2017.06.015. PMID:28648523<ref>PMID:28648523</ref>

~~Description~~:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased~~ Structures]]

</div>

==See Also==

*[[Amylase 3D structures|Amylase 3D structures]]

== References ==

__TOC__

</StructureSection>

[[Category: Large Structures]]

[[Category: Thermotoga petrophila RKU-1]]

[[Category: Hameed U]]

[[Category: Mirza OA]]

[[Category: Price I]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5m99 is ON HOLD
+==Functional Characterization and Crystal Structure of Thermostable Amylase from Thermotoga petrophila, reveals High Thermostability and an Archaic form of Dimerization==
+<StructureSection load='5m99' size='340' side='right'caption='[[5m99]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5m99]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_petrophila_RKU-1 Thermotoga petrophila RKU-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M99 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5M99 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.96&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></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=5m99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m99 OCA], [https://pdbe.org/5m99 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5m99 RCSB], [https://www.ebi.ac.uk/pdbsum/5m99 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5m99 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/A0A059TXD8_THEP1 A0A059TXD8_THEP1]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Thermostable alpha-amylases have many industrial applications and are therefore continuously explored from novel sources. We present the characterization of a novel putative alpha-amylase gene product (Tp-AmyS) cloned from Thermotoga petrophila. The purified recombinant enzyme is highly thermostable and able to hydrolyze starch into dextrin between 90 and 100 degrees C, with optimum activity at 98 degrees C and pH8.5. The activity increased in the presence of Rb1+, K1+ and Ca2+ ions, whereas other ions inhibited activity. The crystal structure of Tp-AmyS at 1.7A resolution showed common features of the GH-13 family, however was apparently found to be a dimer. Several residues from one monomer interacted with a docked acarbose, an inhibitor of Tp-AmyS, in the other monomer, suggesting catalytic cooperativity within the dimer. The most striking feature of the dimer was that it resembled the dimerization of salivary amylase from a previous crystal structure, and thus could be a functional feature of some amylases.
-Authors:
+Functional characterization and crystal structure of thermostable amylase from Thermotoga petrophila, reveals high thermostability and an unusual form of dimerization.,Hameed U, Price I, Ikram-Ul-Haq, Ke A, Wilson DB, Mirza O Biochim Biophys Acta. 2017 Jun 22;1865(10):1237-1245. doi:, 10.1016/j.bbapap.2017.06.015. PMID:28648523<ref>PMID:28648523</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5m99" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Amylase 3D structures|Amylase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Thermotoga petrophila RKU-1]]
+[[Category: Hameed U]]
+[[Category: Mirza OA]]
+[[Category: Price I]]