1o17: Difference between revisions

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[[Image:1o17.png|left|200px]]


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==ANTHRANILATE PHOSPHORIBOSYL-TRANSFERASE (TRPD)==
The line below this paragraph, containing "STRUCTURE_1o17", creates the "Structure Box" on the page.
<StructureSection load='1o17' size='340' side='right'caption='[[1o17]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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>
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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=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>
{{STRUCTURE_1o17|  PDB=1o17  |  SCENE=  }}
</table>
== Function ==
[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]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o1/1o17_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1o17 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


===ANTHRANILATE PHOSPHORIBOSYL-TRANSFERASE (TRPD)===
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<ref>PMID:12093726</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1o17" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_12093726}}, adds the Publication Abstract to the page
*[[Phosphoribosyltransferase 3D structures|Phosphoribosyltransferase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 12093726 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_12093726}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
[[1o17]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus 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].
[[Category: Saccharolobus solfataricus]]
 
[[Category: Ivens A]]
==Reference==
[[Category: Kirschner K]]
<ref group="xtra">PMID:012093726</ref><references group="xtra"/>
[[Category: Mayans O]]
[[Category: Anthranilate phosphoribosyltransferase]]
[[Category: Wilmanns M]]
[[Category: Sulfolobus solfataricus]]
[[Category: Ivens, A.]]
[[Category: Kirschner, K.]]
[[Category: Mayans, O.]]
[[Category: Wilmanns, M.]]
[[Category: Nucleoside-phosphorylase]]
[[Category: Transferase]]

Latest revision as of 02:44, 28 December 2023

ANTHRANILATE PHOSPHORIBOSYL-TRANSFERASE (TRPD)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.

See Also

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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

1o17, resolution 2.05Å

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