8jkr

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(New page: '''Unreleased structure''' The entry 8jkr is ON HOLD Authors: Description: Category: Unreleased Structures)
Current revision (13:14, 21 August 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 8jkr is ON HOLD
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==SP1746 in complex with UMP==
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<StructureSection load='8jkr' size='340' side='right'caption='[[8jkr]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8jkr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_TIGR4 Streptococcus pneumoniae TIGR4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8JKR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8JKR FirstGlance]. <br>
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</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&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8jkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8jkr OCA], [https://pdbe.org/8jkr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8jkr RCSB], [https://www.ebi.ac.uk/pdbsum/8jkr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8jkr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A0A0H2URF8_STRPN A0A0H2URF8_STRPN]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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In this report, we structurally and biochemically characterized the unknown gene product SP1746 from Streptococcus pneumoniae serotype 4. Various crystal structures of SP1746 in the apo form and in complex with different nucleotides were determined. SP1746 is a globular protein, which belongs to the histidine-aspartate (HD) domain superfamily with two Fe(3+) ions in the active site that are coordinated by key active site residues and water molecules. All nucleotides bind in a similar orientation in the active site with their phosphate groups anchored to the diiron cluster. Biochemically, SP1746 hydrolyzes different nucleotide substrates. SP1746 most effectively hydrolyzes diadenosine tetraphosphate (Ap4A) to two ADPs. Based on the aforementioned data, we annotated SP1746 as an Ap4A hydrolase, belonging to the YqeK family. Our in vitro data indicate a potential role for SP1746 in regulating Ap4A homeostasis, which requires validation with in vivo experiments in bacteria in the future.
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Authors:
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Structural and biochemical characterization of a nucleotide hydrolase from Streptococcus pneumonia.,Jin Y, Ke J, Zheng P, Zhang H, Zhu Z, Niu L Structure. 2024 Aug 8;32(8):1197-1207.e4. doi: 10.1016/j.str.2024.04.009. Epub , 2024 May 2. PMID:38701795<ref>PMID:38701795</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 8jkr" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Streptococcus pneumoniae TIGR4]]
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[[Category: Jin Y]]
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[[Category: Ke J]]
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[[Category: Niu L]]

Current revision

SP1746 in complex with UMP

PDB ID 8jkr

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