5zgo: Difference between revisions

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New page: '''Unreleased structure''' The entry 5zgo is ON HOLD Authors: Description: Category: Unreleased Structures
 
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'''Unreleased structure'''


The entry 5zgo is ON HOLD
==Crystal structure of APRT2 from Thermus thermophilus HB8==
<StructureSection load='5zgo' size='340' side='right'caption='[[5zgo]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5zgo]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZGO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZGO 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]] 2.6&#8491;</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=5zgo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zgo OCA], [https://pdbe.org/5zgo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zgo RCSB], [https://www.ebi.ac.uk/pdbsum/5zgo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zgo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5SHW6_THET8 Q5SHW6_THET8]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The present work describes the functional and structural characterization of adenine phosphoribosyltransferase 2 from Thermus thermophilus HB8 (TtAPRT2). The combination of structural and substrate specificity data provided valuable information for immobilization studies. Dimeric TtAPRT2 was immobilized onto glutaraldehyde-activated MagReSyn(R)Amine magnetic iron oxide porous microparticles by two different strategies: a) an enzyme immobilization at pH 8.5 to encourage the immobilization process by N-termini (MTtAPRT2A, MTtAPRT2B, MTtAPRT2C) or b) an enzyme immobilization at pH 10.0 to encourage the immobilization process through surface exposed lysine residues (MTtAPRT2D, MTtAPRT2E, MTtAPRT2F). According to catalyst load experiments, MTtAPRT2B (activity: 480IUg(-1)biocatalyst, activity recovery: 52%) and MTtAPRT2F (activity: 507IUg(-1)biocatalyst, activity recovery: 44%) were chosen as optimal derivatives. The biochemical characterization studies demonstrated that immobilization process improved the thermostability of TtAPRT2. Moreover, the potential reusability of MTtAPRT2B and MTtAPRT2F was also tested. Finally, MTtAPRT2F was employed in the synthesis of nucleoside-5'-monophosphate analogues.


Authors:  
Structural and functional characterization of thermostable biocatalysts for the synthesis of 6-aminopurine nucleoside-5'-monophospate analogues.,Arco JD, Perez E, Naitow H, Matsuura Y, Kunishima N, Fernandez-Lucas J Bioresour Technol. 2019 Mar;276:244-252. doi: 10.1016/j.biortech.2018.12.120., Epub 2019 Jan 3. PMID:30640018<ref>PMID:30640018</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 5zgo" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Phosphoribosyltransferase 3D structures|Phosphoribosyltransferase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermus thermophilus HB8]]
[[Category: Kunishima N]]
[[Category: Matsuura Y]]
[[Category: Naitow H]]

Latest revision as of 11:54, 22 November 2023

Crystal structure of APRT2 from Thermus thermophilus HB8Crystal structure of APRT2 from Thermus thermophilus HB8

Structural highlights

5zgo is a 6 chain structure with sequence from Thermus thermophilus HB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q5SHW6_THET8

Publication Abstract from PubMed

The present work describes the functional and structural characterization of adenine phosphoribosyltransferase 2 from Thermus thermophilus HB8 (TtAPRT2). The combination of structural and substrate specificity data provided valuable information for immobilization studies. Dimeric TtAPRT2 was immobilized onto glutaraldehyde-activated MagReSyn(R)Amine magnetic iron oxide porous microparticles by two different strategies: a) an enzyme immobilization at pH 8.5 to encourage the immobilization process by N-termini (MTtAPRT2A, MTtAPRT2B, MTtAPRT2C) or b) an enzyme immobilization at pH 10.0 to encourage the immobilization process through surface exposed lysine residues (MTtAPRT2D, MTtAPRT2E, MTtAPRT2F). According to catalyst load experiments, MTtAPRT2B (activity: 480IUg(-1)biocatalyst, activity recovery: 52%) and MTtAPRT2F (activity: 507IUg(-1)biocatalyst, activity recovery: 44%) were chosen as optimal derivatives. The biochemical characterization studies demonstrated that immobilization process improved the thermostability of TtAPRT2. Moreover, the potential reusability of MTtAPRT2B and MTtAPRT2F was also tested. Finally, MTtAPRT2F was employed in the synthesis of nucleoside-5'-monophosphate analogues.

Structural and functional characterization of thermostable biocatalysts for the synthesis of 6-aminopurine nucleoside-5'-monophospate analogues.,Arco JD, Perez E, Naitow H, Matsuura Y, Kunishima N, Fernandez-Lucas J Bioresour Technol. 2019 Mar;276:244-252. doi: 10.1016/j.biortech.2018.12.120., Epub 2019 Jan 3. PMID:30640018[1]

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

See Also

References

  1. Arco JD, Perez E, Naitow H, Matsuura Y, Kunishima N, Fernandez-Lucas J. Structural and functional characterization of thermostable biocatalysts for the synthesis of 6-aminopurine nucleoside-5'-monophospate analogues. Bioresour Technol. 2019 Mar;276:244-252. doi: 10.1016/j.biortech.2018.12.120., Epub 2019 Jan 3. PMID:30640018 doi:http://dx.doi.org/10.1016/j.biortech.2018.12.120

5zgo, resolution 2.60Å

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