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==Crystal structure of hypothetical protein PF0907 from pyrococcus furiosus solved by sulfur SAD using Swiss light source data==
==Crystal structure of hypothetical protein PF0907 from pyrococcus furiosus solved by sulfur SAD using Swiss light source data==
<StructureSection load='4pii' size='340' side='right' caption='[[4pii]], [[Resolution|resolution]] 2.17&Aring;' scene=''>
<StructureSection load='4pii' size='340' side='right'caption='[[4pii]], [[Resolution|resolution]] 2.17&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4pii]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrfu Pyrfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PII OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PII FirstGlance]. <br>
<table><tr><td colspan='2'>[[4pii]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus_DSM_3638 Pyrococcus furiosus DSM 3638]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PII OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PII FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></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]] 2.17&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1xg7|1xg7]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PF0904 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186497 PYRFU])</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=4pii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pii OCA], [https://pdbe.org/4pii PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pii RCSB], [https://www.ebi.ac.uk/pdbsum/4pii PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pii ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pii OCA], [http://pdbe.org/4pii PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pii RCSB], [http://www.ebi.ac.uk/pdbsum/4pii PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pii ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/AGOG_PYRFU AGOG_PYRFU]] DNA repair enzyme that is part of the base excision repair (BER) pathway; protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine (GO), from single- and double-stranded DNA substrates (By similarity).  
[https://www.uniprot.org/uniprot/AGOG_PYRFU AGOG_PYRFU] DNA repair enzyme that is part of the base excision repair (BER) pathway; protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine (GO), from single- and double-stranded DNA substrates (By similarity).
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 4pii" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4pii" style="background-color:#fffaf0;"></div>
==See Also==
*[[DNA glycosylase 3D structures|DNA glycosylase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Pyrfu]]
[[Category: Large Structures]]
[[Category: Chen, L]]
[[Category: Pyrococcus furiosus DSM 3638]]
[[Category: Olieric, V]]
[[Category: Chen L]]
[[Category: Panepucci, E]]
[[Category: Olieric V]]
[[Category: Rose, J P]]
[[Category: Panepucci E]]
[[Category: Structural genomic]]
[[Category: Rose JP]]
[[Category: Waltersperger, S]]
[[Category: Waltersperger S]]
[[Category: Wang, B C]]
[[Category: Wang BC]]
[[Category: Wang, M]]
[[Category: Wang M]]
[[Category: Weinert, T]]
[[Category: Weinert T]]
[[Category: Secsg]]
[[Category: Sulfur sad]]
[[Category: Unknown function]]

Latest revision as of 03:44, 28 December 2023

Crystal structure of hypothetical protein PF0907 from pyrococcus furiosus solved by sulfur SAD using Swiss light source dataCrystal structure of hypothetical protein PF0907 from pyrococcus furiosus solved by sulfur SAD using Swiss light source data

Structural highlights

4pii is a 1 chain structure with sequence from Pyrococcus furiosus DSM 3638. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.17Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AGOG_PYRFU DNA repair enzyme that is part of the base excision repair (BER) pathway; protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine (GO), from single- and double-stranded DNA substrates (By similarity).

Publication Abstract from PubMed

We describe a data collection method that uses a single crystal to solve X-ray structures by native SAD (single-wavelength anomalous diffraction). We solved the structures of 11 real-life examples, including a human membrane protein, a protein-DNA complex and a 266-kDa multiprotein-ligand complex, using this method. The data collection strategy is suitable for routine structure determination and can be implemented at most macromolecular crystallography synchrotron beamlines.

Fast native-SAD phasing for routine macromolecular structure determination.,Weinert T, Olieric V, Waltersperger S, Panepucci E, Chen L, Zhang H, Zhou D, Rose J, Ebihara A, Kuramitsu S, Li D, Howe N, Schnapp G, Pautsch A, Bargsten K, Prota AE, Surana P, Kottur J, Nair DT, Basilico F, Cecatiello V, Pasqualato S, Boland A, Weichenrieder O, Wang B, Steinmetz MO, Caffrey M, Wang M Nat Methods. 2014 Dec 15. doi: 10.1038/nmeth.3211. PMID:25506719[1]

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

See Also

References

  1. Weinert T, Olieric V, Waltersperger S, Panepucci E, Chen L, Zhang H, Zhou D, Rose J, Ebihara A, Kuramitsu S, Li D, Howe N, Schnapp G, Pautsch A, Bargsten K, Prota AE, Surana P, Kottur J, Nair DT, Basilico F, Cecatiello V, Pasqualato S, Boland A, Weichenrieder O, Wang B, Steinmetz MO, Caffrey M, Wang M. Fast native-SAD phasing for routine macromolecular structure determination. Nat Methods. 2014 Dec 15. doi: 10.1038/nmeth.3211. PMID:25506719 doi:http://dx.doi.org/10.1038/nmeth.3211

4pii, resolution 2.17Å

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OCA