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1o17

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ANTHRANILATE PHOSPHORIBOSYL-TRANSFERASE (TRPD)

Structural highlights

1o17 is a 4 chain structure with sequence from Saccharolobus solfataricus. This structure supersedes the now removed PDB entry 1k8e. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.05Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TRPD_SACS2 Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).[HAMAP-Rule:MF_00211]^[1] ^[2]

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 crystal structure of the dimeric anthranilate phosphoribosyltransferase (AnPRT) reveals a new category of phosphoribosyltransferases, designated as class III. The active site of this enzyme is located within the flexible hinge region of its two-domain structure. The pyrophosphate moiety of phosphoribosylpyrophosphate is co-ordinated by a metal ion and is bound by two conserved loop regions within this hinge region. With the structure of AnPRT available, structural analysis of all enzymatic activities of the tryptophan biosynthesis pathway is complete, thereby connecting the evolution of its enzyme members to the general development of metabolic processes. Its structure reveals it to have the same fold, topology, active site location and type of association as class II nucleoside phosphorylases. At the level of sequences, this relationship is mirrored by 13 structurally invariant residues common to both enzyme families. Taken together, these data imply common ancestry of enzymes catalysing reverse biological processes--the ribosylation and deribosylation of metabolic pathway intermediates. These relationships establish new links for enzymes involved in nucleotide and amino acid metabolism.

Structural analysis of two enzymes catalysing reverse metabolic reactions implies common ancestry.,Mayans O, Ivens A, Nissen LJ, Kirschner K, Wilmanns M EMBO J. 2002 Jul 1;21(13):3245-54. PMID:12093726^[3]

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

References

↑ Ivens A, Mayans O, Szadkowski H, Wilmanns M, Kirschner K. Purification, characterization and crystallization of thermostable anthranilate phosphoribosyltransferase from Sulfolobus solfataricus. Eur J Biochem. 2001 Apr;268(8):2246-52. PMID:11298741
↑ Marino M, Deuss M, Svergun DI, Konarev PV, Sterner R, Mayans O. Structural and mutational analysis of substrate complexation by anthranilate phosphoribosyltransferase from Sulfolobus solfataricus. J Biol Chem. 2006 Jul 28;281(30):21410-21. Epub 2006 May 19. PMID:16714288 doi:10.1074/jbc.M601403200
↑ Mayans O, Ivens A, Nissen LJ, Kirschner K, Wilmanns M. Structural analysis of two enzymes catalysing reverse metabolic reactions implies common ancestry. EMBO J. 2002 Jul 1;21(13):3245-54. PMID:12093726 doi:http://dx.doi.org/10.1093/emboj/cdf298

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1o17"

@@ Line 3: / Line 3: @@
 <StructureSection load='1o17' size='340' side='right'caption='[[1o17]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1o17]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_35091 Atcc 35091]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1k8e 1k8e]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O17 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O17 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1o17]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1k8e 1k8e]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O17 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O17 FirstGlance]. <br>
-</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Anthranilate_phosphoribosyltransferase Anthranilate phosphoribosyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.18 2.4.2.18] </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]] 2.05&#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=1o17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o17 OCA], [https://pdbe.org/1o17 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o17 RCSB], [https://www.ebi.ac.uk/pdbsum/1o17 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o17 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/TRPD_SULSO TRPD_SULSO]] Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).<ref>PMID:11298741</ref> <ref>PMID:16714288</ref>
+[https://www.uniprot.org/uniprot/TRPD_SACS2 TRPD_SACS2] Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).[HAMAP-Rule:MF_00211]<ref>PMID:11298741</ref> <ref>PMID:16714288</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 35: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Anthranilate phosphoribosyltransferase]]
-[[Category: Atcc 35091]]
 [[Category: Large Structures]]
-[[Category: Ivens, A]]
+[[Category: Saccharolobus solfataricus]]
-[[Category: Kirschner, K]]
+[[Category: Ivens A]]
-[[Category: Mayans, O]]
+[[Category: Kirschner K]]
-[[Category: Wilmanns, M]]
+[[Category: Mayans O]]
-[[Category: Nucleoside-phosphorylase]]
+[[Category: Wilmanns M]]
-[[Category: Transferase]]

1o17

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Current revision

ANTHRANILATE PHOSPHORIBOSYL-TRANSFERASE (TRPD)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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