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2x30

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Revision as of 19:06, 24 January 2018

Crystal structure of the r139n mutant of a bifunctional enzyme pria

Structural highlights

2x30 is a 1 chain structure with sequence from "actinomyces_coelicolor"_(muller_1908)_lieske_1921 "actinomyces coelicolor" (muller 1908) lieske 1921. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2vep, 1vzw
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[HIS4_STRCO] Catalyzes the isomerization of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR in the biosynthesis pathway for histidine and the isomerization of the aminoaldose PRA to the aminoketose CdRP in the biosynthsis pathway for tryptophan.[HAMAP-Rule:MF_01014]

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

A good model to experimentally explore evolutionary hypothesis related to enzyme function is the ancient-like dual-substrate (betaalpha)(8) phosphoribosyl isomerase (PriA), which takes part in both histidine and tryptophan biosynthesis in Streptomyces coelicolor and related organisms. In this study, we determined the Michaelis - Menten enzyme kinetics for both isomerase activities in wild-type PriA from S. coelicolor, as well as in selected single-residue mono-functional mutants, identified after Escherichia coli in vivo complementation experiments. Structural and functional analyses of a hitherto unnoticed residue contained on the functionally important beta --> alpha loop 5, namely, Arg(139), which was postulated on structural grounds to be important for the dual-substrate specificity of PriA, is presented for the first time. Indeed, enzyme kinetics analyses done on the mutant variants PriA_Ser(81)Thr and PriA_Arg(139)Asn showed that these residues, which are contained on beta --> alpha loops and in close proximity to the N-terminal phosphate-binding site, are essential solely for the phosphoribosyl anthranilate isomerase activity of PriA. Moreover, analysis of the X-ray crystallographic structure of PriA_Arg(139)Asn elucidated at 1.95 A herein, strongly implicates the occurrence of conformational changes in this beta --> alpha loop as a major structural feature related to the evolution of the dual-substrate specificity of PriA. It is suggested that PriA has evolved by tuning a fine energetic balance that allows the sufficient degree of structural flexibility needed for accommodating two topologically dissimilar substrates - within a bifunctional and thus highly constrained active site - without compromising its structural stability.

Identification and analysis of residues contained on beta --> alpha loops of the dual-substrate (betaalpha)(8) phosphoribosyl isomerase a (PriA) specific for its phosphoribosyl anthranilate isomerase activity.,Noda-Garcia L, Camacho-Zarco AR, Verdel-Aranda K, Wright H, Soberon X, Fulop V, Barona-Gomez F Protein Sci. 2010 Jan 11. PMID:20066665^[1]

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

References

↑ Noda-Garcia L, Camacho-Zarco AR, Verdel-Aranda K, Wright H, Soberon X, Fulop V, Barona-Gomez F. Identification and analysis of residues contained on beta --> alpha loops of the dual-substrate (betaalpha)(8) phosphoribosyl isomerase a (PriA) specific for its phosphoribosyl anthranilate isomerase activity. Protein Sci. 2010 Jan 11. PMID:20066665 doi:10.1002/pro.331

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2x30"

@@ Line 1: / Line 1: @@
-==CRYSTAL STRUCTURE OF THE R139N MUTANT OF A BIFUNCTIONAL ENZYME PRIA==
+==Crystal structure of the r139n mutant of a bifunctional enzyme pria==
 <StructureSection load='2x30' size='340' side='right' caption='[[2x30]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
 == Structural highlights ==
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vep|2vep]], [[1vzw|1vzw]]</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=2x30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x30 OCA], [http://pdbe.org/2x30 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2x30 RCSB], [http://www.ebi.ac.uk/pdbsum/2x30 PDBsum]</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=2x30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x30 OCA], [http://pdbe.org/2x30 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2x30 RCSB], [http://www.ebi.ac.uk/pdbsum/2x30 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2x30 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x3/2x30_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x3/2x30_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2x30

From Proteopedia

Revision as of 19:06, 24 January 2018

Crystal structure of the r139n mutant of a bifunctional enzyme pria

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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