4d8x: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4d8x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D8X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D8X FirstGlance]. <br>
<table><tr><td colspan='2'>[[4d8x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D8X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D8X FirstGlance]. <br>
</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=4d8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d8x OCA], [https://pdbe.org/4d8x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d8x RCSB], [https://www.ebi.ac.uk/pdbsum/4d8x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d8x ProSAT]</span></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]] 2.65&#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=4d8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d8x OCA], [https://pdbe.org/4d8x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d8x RCSB], [https://www.ebi.ac.uk/pdbsum/4d8x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d8x ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/DEOD_BACSU DEOD_BACSU]] Cleavage of adenosine and its derivatives.
[https://www.uniprot.org/uniprot/DEOD_BACSU DEOD_BACSU] Cleavage of adenosine and its derivatives.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The hexameric purine nucleoside phosphorylase from Bacillus subtilis (BsPNP233) displays great potential to produce nucleoside analogues in industry and can be exploited in the development of new anti-tumor gene therapies. In order to provide structural basis for enzyme and substrates rational optimization, aiming at those applications, the present work shows a thorough and detailed structural description of the binding mode of substrates and nucleoside analogues to the active site of the hexameric BsPNP233. Here we report the crystal structure of BsPNP233 in the apo form and in complex with 11 ligands, including clinically relevant compounds. The crystal structure of six ligands (adenine, 2'deoxyguanosine, aciclovir, ganciclovir, 8-bromoguanosine, 6-chloroguanosine) in complex with a hexameric PNP are presented for the first time. Our data showed that free bases adopt alternative conformations in the BsPNP233 active site and indicated that binding of the co-substrate (2'deoxy)ribose 1-phosphate might contribute for stabilizing the bases in a favorable orientation for catalysis. The BsPNP233-adenosine complex revealed that a hydrogen bond between the 5' hydroxyl group of adenosine and Arg(43*) side chain contributes for the ribosyl radical to adopt an unusual C3'-endo conformation. The structures with 6-chloroguanosine and 8-bromoguanosine pointed out that the Cl(6) and Br(8) substrate modifications seem to be detrimental for catalysis and can be explored in the design of inhibitors for hexameric PNPs from pathogens. Our data also corroborated the competitive inhibition mechanism of hexameric PNPs by tubercidin and suggested that the acyclic nucleoside ganciclovir is a better inhibitor for hexameric PNPs than aciclovir. Furthermore, comparative structural analyses indicated that the replacement of Ser(90) by a threonine in the B. cereus hexameric adenosine phosphorylase (Thr(91)) is responsible for the lack of negative cooperativity of phosphate binding in this enzyme.
 
Insights into phosphate cooperativity and influence of substrate modifications on binding and catalysis of hexameric purine nucleoside phosphorylases.,de Giuseppe PO, Martins NH, Meza AN, Dos Santos CR, Pereira HD, Murakami MT PLoS One. 2012;7(9):e44282. Epub 2012 Sep 5. PMID:22957058<ref>PMID:22957058</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4d8x" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Purine nucleoside phosphorylase 3D structures|Purine nucleoside phosphorylase 3D structures]]
*[[Purine nucleoside phosphorylase 3D structures|Purine nucleoside phosphorylase 3D structures]]
== References ==
<references/>
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__TOC__
</StructureSection>
</StructureSection>

Latest revision as of 13:42, 1 March 2024

Crystal structure of the hexameric purine nucleoside phosphorylase from Bacillus subtilis in space group P6322 at pH 4.6Crystal structure of the hexameric purine nucleoside phosphorylase from Bacillus subtilis in space group P6322 at pH 4.6

Structural highlights

4d8x is a 1 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.65Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DEOD_BACSU Cleavage of adenosine and its derivatives.

See Also

4d8x, resolution 2.65Å

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