5hkf

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of Mycobacterium tuberculosis H37Rv orotate phosphoribosyltransferase in complex with 5-phospho-alpha-D-ribosyl 1-diphosphate (PRPP)

Structural highlights

5hkf is a 2 chain structure with sequence from Mycobacterium tuberculosis H37Rv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.25Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PYRE_MYCTU Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).

Publication Abstract from PubMed

The Mycobacterium tuberculosis orotate phosphoribosyltransferase (MtOPRT) catalyses the conversion of alpha-D-5-phosphoribosyl-1-pyrophosphate (PRPP) and orotate (OA) in pyrophosphate and orotidine 5'-monophosphate (OMP), in presence of Mg(2+). This enzyme is the only responsible for the synthesis of orotidine 5'-monophosphate, a key precursor in the de novo pyrimidine biosynthesis pathway, making MtOPRT an attractive drug target for the development of antitubercular agents. We report the crystal structures of MtOPRT in complex with PRPP (2.25 A resolution), inorganic phosphate (1.90 A resolution) and the exogenous compound Fe(III) dicitrate (2.40 A resolution). The overall structure of the mycobacterial enzyme is highly similar to those described for other OPRTases, with the "flexible loop" assuming a well define conformation and making specific contacts with the Fe(III)-dicitrate complex. The structures here reported add to the knowledge of a potential drug target for tuberculosis, and will provide a useful tool for the structure-based drug design of potent enzyme inhibitors.

Structural investigations on orotate phosphoribosyltransferase from Mycobacterium tuberculosis, a key enzyme of the de novo pyrimidine biosynthesis.,Donini S, Ferraris DM, Miggiano R, Massarotti A, Rizzi M Sci Rep. 2017 Apr 26;7(1):1180. doi: 10.1038/s41598-017-01057-z. PMID:28446777^[1]

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

References

↑ Donini S, Ferraris DM, Miggiano R, Massarotti A, Rizzi M. Structural investigations on orotate phosphoribosyltransferase from Mycobacterium tuberculosis, a key enzyme of the de novo pyrimidine biosynthesis. Sci Rep. 2017 Apr 26;7(1):1180. doi: 10.1038/s41598-017-01057-z. PMID:28446777 doi:http://dx.doi.org/10.1038/s41598-017-01057-z

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5hkf"

@@ Line 1: / Line 1: @@
 ==Crystal structure of Mycobacterium tuberculosis H37Rv orotate phosphoribosyltransferase in complex with 5-phospho-alpha-D-ribosyl 1-diphosphate (PRPP)==
-<StructureSection load='5hkf' size='340' side='right' caption='[[5hkf]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
+<StructureSection load='5hkf' size='340' side='right'caption='[[5hkf]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5hkf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HKF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HKF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5hkf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HKF FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PRP:ALPHA-PHOSPHORIBOSYLPYROPHOSPHORIC+ACID'>PRP</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]] 2.25&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pyrE, umpA, Rv0382c, MTV036.17c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PRP:ALPHA-PHOSPHORIBOSYLPYROPHOSPHORIC+ACID'>PRP</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Orotate_phosphoribosyltransferase Orotate phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.10 2.4.2.10] </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=5hkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hkf OCA], [https://pdbe.org/5hkf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hkf RCSB], [https://www.ebi.ac.uk/pdbsum/5hkf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hkf 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=5hkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hkf OCA], [http://pdbe.org/5hkf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hkf RCSB], [http://www.ebi.ac.uk/pdbsum/5hkf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hkf ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PYRE_MYCTU PYRE_MYCTU]] Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
+[https://www.uniprot.org/uniprot/PYRE_MYCTU PYRE_MYCTU] Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 19: @@
 </div>
 <div class="pdbe-citations 5hkf" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Phosphoribosyltransferase 3D structures|Phosphoribosyltransferase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Myctu]]
+[[Category: Large Structures]]
-[[Category: Orotate phosphoribosyltransferase]]
+[[Category: Mycobacterium tuberculosis H37Rv]]
-[[Category: Bolognesi, G]]
+[[Category: Bolognesi G]]
-[[Category: Donini, S]]
+[[Category: Donini S]]
-[[Category: Ferraris, D M]]
+[[Category: Ferraris DM]]
-[[Category: Rizzi, M]]
+[[Category: Rizzi M]]
-[[Category: De novo pyrimidine nucleotide synthesis]]
-[[Category: Oprt]]
-[[Category: Prpp complex]]
-[[Category: Transferase]]

5hkf

From Proteopedia

Current revision

Crystal structure of Mycobacterium tuberculosis H37Rv orotate phosphoribosyltransferase in complex with 5-phospho-alpha-D-ribosyl 1-diphosphate (PRPP)

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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