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| | ==X-ray crystal structure of Chlamydia trachomatis Mn(II)Fe(II)-NrdB== | | ==X-ray crystal structure of Chlamydia trachomatis Mn(II)Fe(II)-NrdB== |
| - | <StructureSection load='4m1i' size='340' side='right' caption='[[4m1i]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='4m1i' size='340' side='right'caption='[[4m1i]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4m1i]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"chlamydozoon_trachomatis"_(busacca_1935)_moshkovski_1945 "chlamydozoon trachomatis" (busacca 1935) moshkovski 1945]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M1I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4M1I FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4m1i]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydia_trachomatis Chlamydia trachomatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M1I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M1I FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4m1h|4m1h]]</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=4m1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m1i OCA], [https://pdbe.org/4m1i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m1i RCSB], [https://www.ebi.ac.uk/pdbsum/4m1i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m1i ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CT_828, nrdB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=813 "Chlamydozoon trachomatis" (Busacca 1935) Moshkovski 1945])</td></tr>
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| - | <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>
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| - | <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=4m1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m1i OCA], [http://pdbe.org/4m1i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4m1i RCSB], [http://www.ebi.ac.uk/pdbsum/4m1i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4m1i ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RIR2_CHLTR RIR2_CHLTR]] Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity). | + | [https://www.uniprot.org/uniprot/RIR2_CHLTR RIR2_CHLTR] Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Ribonucleotide reductase|Ribonucleotide reductase]] | + | *[[Ribonucleotide reductase 3D structures|Ribonucleotide reductase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ribonucleoside-diphosphate reductase]] | + | [[Category: Chlamydia trachomatis]] |
| - | [[Category: Boal, A K]] | + | [[Category: Large Structures]] |
| - | [[Category: Rosenzweig, A C]] | + | [[Category: Boal AK]] |
| - | [[Category: Oxidoreductase]] | + | [[Category: Rosenzweig AC]] |
| - | [[Category: Ribonucleotide reductase]]
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| Structural highlights
Function
RIR2_CHLTR Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity).
Publication Abstract from PubMed
The class Ic ribonucleotide reductase (RNR) from Chlamydia trachomatis (Ct) employs a MnIV/FeIII cofactor in each monomer of its beta2 subunit to initiate nucleotide reduction. The cofactor forms by reaction of MnII/FeII-beta2 with O2. Previously, in vitro cofactor assembly from apo beta2 and divalent metal ions produced a mixture of two forms, with Mn in site 1 (MnIV/FeIII) or site 2 (FeIII/MnIV), of which the more active MnIV/FeIII product predominates. Here we have addressed the basis for metal site-selectivity by solving X-ray crystal structures of apo, MnII, and MnII/FeII complexes of Ct beta2. A structure obtained anaerobically with equimolar MnII, FeII, and apo protein reveals exclusive incorporation of MnII in site 1 and FeII in site 2, in contrast to the more modest site-selectivity achieved previously. Site-specificity is controlled thermodynamically by the apo protein structure, as only minor adjustments of ligands occur upon metal binding. Additional structures imply that, by itself, MnII binds in either site. Together the structures are consistent with a model for in vitro cofactor assembly in which FeII specificity for site 2 drives assembly of the appropriately configured heterobimetallic center, provided that FeII is substoichiometric. This model suggests that use of an MnIV/FeIII cofactor in vivo could be an adaptation to FeII limitation. A 1.8 A resolution model of the MnII/FeII-beta2 complex reveals additional structural determinants for activation of the cofactor, including a proposed site for side-on (eta2) addition of O2 to FeII and a short (3.2 A) MnII-FeII interionic distance, promoting formation of the MnIV/FeIV activation intermediate.
Structural Basis for Assembly of the Mn/Fe Cofactor in the Class Ic Ribonucleotide Reductase from Chlamydia trachomatis.,Dassama LM, Krebs C, Bollinger JM, Rosenzweig AC, Boal AK Biochemistry. 2013 Aug 7. PMID:23924396[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dassama LM, Krebs C, Bollinger JM, Rosenzweig AC, Boal AK. Structural Basis for Assembly of the Mn/Fe Cofactor in the Class Ic Ribonucleotide Reductase from Chlamydia trachomatis. Biochemistry. 2013 Aug 7. PMID:23924396 doi:10.1021/bi400819x
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