2f8m: Difference between revisions

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<StructureSection load='2f8m' size='340' side='right'caption='[[2f8m]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
<StructureSection load='2f8m' size='340' side='right'caption='[[2f8m]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2f8m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Plaf7 Plaf7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F8M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F8M FirstGlance]. <br>
<table><tr><td colspan='2'>[[2f8m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_3D7 Plasmodium falciparum 3D7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F8M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F8M FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.087&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PFE0730c ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=36329 PLAF7])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ribose-5-phosphate_isomerase Ribose-5-phosphate isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.6 5.3.1.6] </span></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=2f8m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f8m OCA], [https://pdbe.org/2f8m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f8m RCSB], [https://www.ebi.ac.uk/pdbsum/2f8m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f8m ProSAT]</span></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=2f8m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f8m OCA], [https://pdbe.org/2f8m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f8m RCSB], [https://www.ebi.ac.uk/pdbsum/2f8m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f8m ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RPIA_PLAF7 RPIA_PLAF7] Involved in the first step of the non-oxidative branch of the pentose phosphate pathway. It catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.[UniProtKB:P0A7Z0]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Plaf7]]
[[Category: Plasmodium falciparum 3D7]]
[[Category: Ribose-5-phosphate isomerase]]
[[Category: Holmes MA]]
[[Category: Holmes, M A]]
[[Category: Merritt EA]]
[[Category: Merritt, E A]]
[[Category: Structural genomic]]
[[Category: Isomerase]]
[[Category: PSI, Protein structure initiative]]
[[Category: Sgpp]]

Latest revision as of 12:22, 30 August 2023

Ribose 5-phosphate isomerase from Plasmodium falciparumRibose 5-phosphate isomerase from Plasmodium falciparum

Structural highlights

2f8m is a 2 chain structure with sequence from Plasmodium falciparum 3D7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.087Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RPIA_PLAF7 Involved in the first step of the non-oxidative branch of the pentose phosphate pathway. It catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.[UniProtKB:P0A7Z0]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The structure of ribose 5-phosphate isomerase from Plasmodium falciparum, PFE0730c, has been determined by molecular replacement at 2.09 angstroms resolution. The enzyme, which catalyzes the isomerization reaction that interconverts ribose 5-phosphate and ribulose 5-phosphate, is a member of the pentose phosphate pathway. The P. falciparum enzyme belongs to the ribose 5-phosphate isomerase A family, Pfam family PF06562 (DUF1124), and is structurally similar to other members of the family.

Structure of ribose 5-phosphate isomerase from Plasmodium falciparum.,Holmes MA, Buckner FS, Van Voorhis WC, Verlinde CL, Mehlin C, Boni E, DeTitta G, Luft J, Lauricella A, Anderson L, Kalyuzhniy O, Zucker F, Schoenfeld LW, Earnest TN, Hol WG, Merritt EA Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 May 1;62(Pt, 5):427-31. Epub 2006 Apr 12. PMID:16682767[1]

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

See Also

References

  1. Holmes MA, Buckner FS, Van Voorhis WC, Verlinde CL, Mehlin C, Boni E, DeTitta G, Luft J, Lauricella A, Anderson L, Kalyuzhniy O, Zucker F, Schoenfeld LW, Earnest TN, Hol WG, Merritt EA. Structure of ribose 5-phosphate isomerase from Plasmodium falciparum. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 May 1;62(Pt, 5):427-31. Epub 2006 Apr 12. PMID:16682767 doi:10.1107/S1744309106010876

2f8m, resolution 2.09Å

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