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2xap

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Revision as of 09:05, 5 August 2016

RIBONUCLEOTIDE REDUCTASE Y731NO2Y MODIFIED R1 SUBUNIT OF E. COLI TO 2.1 A RESOLUTION

Structural highlights

2xap is a 7 chain structure with sequence from Ecoli. This structure supersedes the now removed PDB entry 2x1y. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	1r1r, 7r1r, 3r1r, 2r1r, 1qfn, 4r1r, 5r1r, 6r1r, 2xak, 1rlr, 2x0x, 2xaz, 2xav, 2xax, 2xay, 2xaw
Activity:	Ribonucleoside-diphosphate reductase, with EC number 1.17.4.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RIR1_ECOLI] Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R1 contains the binding sites for both substrates and allosteric effectors and carries out the actual reduction of the ribonucleotide. It also provides redox-active cysteines. [RIR2_ECOLI] Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R2 contains the tyrosyl radical required for catalysis.

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

E. coli ribonucleotide reductase catalyzes the reduction of nucleoside 5'-diphosphates into 2'-deoxynucleotides and is composed of two subunits: alpha2 and beta2. During turnover, a stable tyrosyl radical (Y*) at Y(122)-beta2 reversibly oxidizes C(439) in the active site of alpha2. This radical propagation step is proposed to occur over 35 A, to use specific redox-active tyrosines (Y(122) and Y(356) in beta2, Y(731) and Y(730) in alpha2), and to involve proton-coupled electron transfer (PCET). 3-Nitrotyrosine (NO(2)Y, pK(a) 7.1) has been incorporated in place of Y(122), Y(731), and Y(730) to probe how the protein environment perturbs each pK(a) in the presence of the second subunit, substrate (S), and allosteric effector (E). The activity of each mutant is <4 x 10(-3) that of the wild-type (wt) subunit. The [NO(2)Y(730)]-alpha2 and [NO(2)Y(731)]-alpha2 each exhibit a pK(a) of 7.8-8.0 with E and E/beta2. The pK(a) of [NO(2)Y(730)]-alpha2 is elevated to 8.2-8.3 in the S/E/beta2 complex, whereas no further perturbation is observed for [NO(2)Y(731)]-alpha2. Mutations in pathway residues adjacent to the NO(2)Y that disrupt H-bonding minimally perturb its pK(a). The pK(a) of NO(2)Y(122)-beta2 alone or with alpha2/S/E is >9.6. X-ray crystal structures have been obtained for all [NO(2)Y]-alpha2 mutants (2.1-3.1 A resolution), which show minimal structural perturbation compared to wt-alpha2. Together with the pK(a) of the previously reported NO(2)Y(356)-beta2 (7.5 in the alpha2/S/E complex; Yee, C. et al. Biochemistry 2003, 42, 14541-14552), these studies provide a picture of the protein environment of the ground state at each Y in the PCET pathway, and are the starting point for understanding differences in PCET mechanisms at each residue in the pathway.

Site-Specific Incorporation of 3-Nitrotyrosine as a Probe of pK(a) Perturbation of Redox-Active Tyrosines in Ribonucleotide Reductase.,Yokoyama K, Uhlin U, Stubbe J J Am Chem Soc. 2010 Jun 2. PMID:20518462^[1]

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

References

↑ Yokoyama K, Uhlin U, Stubbe J. Site-Specific Incorporation of 3-Nitrotyrosine as a Probe of pK(a) Perturbation of Redox-Active Tyrosines in Ribonucleotide Reductase. J Am Chem Soc. 2010 Jun 2. PMID:20518462 doi:10.1021/ja101097p

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/2xap"

@@ Line 1: / Line 1: @@
 ==RIBONUCLEOTIDE REDUCTASE Y731NO2Y MODIFIED R1 SUBUNIT OF E. COLI TO 2.1 A RESOLUTION==
 <StructureSection load='2xap' size='340' side='right' caption='[[2xap]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2xap]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2x1y 2x1y]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XAP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XAP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2xap]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2x1y 2x1y]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XAP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XAP FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NIY:META-NITRO-TYROSINE'>NIY</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1r1r|1r1r]], [[7r1r|7r1r]], [[3r1r|3r1r]], [[2r1r|2r1r]], [[1qfn|1qfn]], [[4r1r|4r1r]], [[5r1r|5r1r]], [[6r1r|6r1r]], [[2xak|2xak]], [[1rlr|1rlr]], [[2x0x|2x0x]], [[2xaz|2xaz]], [[2xav|2xav]], [[2xax|2xax]], [[2xay|2xay]], [[2xaw|2xaw]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribonucleoside-diphosphate_reductase Ribonucleoside-diphosphate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.4.1 1.17.4.1] </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=2xap FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xap OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xap RCSB], [http://www.ebi.ac.uk/pdbsum/2xap 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=2xap FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xap OCA], [http://pdbe.org/2xap PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xap RCSB], [http://www.ebi.ac.uk/pdbsum/2xap PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xap ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
     <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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=2xap ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 28: / Line 29: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2xap" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 36: / Line 38: @@
 __TOC__
 </StructureSection>
-[[Category: Escherichia coli]]
+[[Category: Ecoli]]
 [[Category: Ribonucleoside-diphosphate reductase]]
 [[Category: Stubbe, J]]

2xap

From Proteopedia

Revision as of 09:05, 5 August 2016

RIBONUCLEOTIDE REDUCTASE Y731NO2Y MODIFIED R1 SUBUNIT OF E. COLI TO 2.1 A RESOLUTION

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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