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[[Image: | ==C85S GAPDX, NMR, 20 STRUCTURES== | ||
<StructureSection load='1gpx' size='340' side='right' caption='[[1gpx]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1gpx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GPX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GPX FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GA:GALLIUM+(III)+ION'>GA</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CAMB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 Pseudomonas putida])</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gpx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gpx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gpx RCSB], [http://www.ebi.ac.uk/pdbsum/1gpx PDBsum]</span></td></tr> | |||
<table> | |||
== 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/gp/1gpx_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/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The Fe2S2 cluster of the ferredoxin putidaredoxin (Pdx) can be replaced by a single gallium ion, giving rise to a colorless, diamagnetic protein in which, apart from the metal binding site, the major structural features of the native ferredoxin are conserved. The solution structure of the C85S variant of gallium putidaredoxin (C85S GaPdx), in which a non-ligand cysteine is replaced by a serine, has been determined via multidimensional NMR methods using uniformly 15N, 13C labeled samples of C85S GaPdx. Stereospecific assignments of leucine and valine methyl resonances were made using 13C, 1H HSQC spectra obtained with fractionally 13C-labeled samples, and backbone dihedral angle restraints were obtained using a combination of two-dimensional J-modulated 15N, 1H HSQC and three-dimensional (HN)CO(CO)NH experiments. A total of 1117 NOE-derived distance restraints were used in the calculations, including 454 short range (i-j < or = 3), 456 long range (i-j > or = 4) interresidue restraints and 207 non-trivial intraresidue restraints. 97 phi and 55 chi 1 angular restraints were also included in the calculation of a family of 20 structures using a combined distance geometry-simulated annealing protocol. Most regions of the protein are well defined in the calculations, with an RMSD of 0.525 A for backbone atoms excluding the metal binding loop (residues 34-48) and the last three C-terminal residues (residues 103-106). Where comparison is possible, these regions show an increase in dynamic behavior over the native protein, as does the loop containing residues 74-76. Structural and dynamic differences between native Pdx and GaPdx are discussed in relation to charge and packing of the metal binding site. | |||
The solution structure of a gallium-substituted putidaredoxin mutant: GaPdx C85S.,Pochapsky TC, Kuti M, Kazanis S J Biomol NMR. 1998 Oct;12(3):407-15. PMID:9835048<ref>PMID:9835048</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Ferredoxin|Ferredoxin]] | *[[Ferredoxin|Ferredoxin]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Pseudomonas putida]] | [[Category: Pseudomonas putida]] | ||
[[Category: Kazanis, S.]] | [[Category: Kazanis, S.]] | ||
Revision as of 16:59, 28 September 2014
C85S GAPDX, NMR, 20 STRUCTURESC85S GAPDX, NMR, 20 STRUCTURES
Structural highlights
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 PubMedThe Fe2S2 cluster of the ferredoxin putidaredoxin (Pdx) can be replaced by a single gallium ion, giving rise to a colorless, diamagnetic protein in which, apart from the metal binding site, the major structural features of the native ferredoxin are conserved. The solution structure of the C85S variant of gallium putidaredoxin (C85S GaPdx), in which a non-ligand cysteine is replaced by a serine, has been determined via multidimensional NMR methods using uniformly 15N, 13C labeled samples of C85S GaPdx. Stereospecific assignments of leucine and valine methyl resonances were made using 13C, 1H HSQC spectra obtained with fractionally 13C-labeled samples, and backbone dihedral angle restraints were obtained using a combination of two-dimensional J-modulated 15N, 1H HSQC and three-dimensional (HN)CO(CO)NH experiments. A total of 1117 NOE-derived distance restraints were used in the calculations, including 454 short range (i-j < or = 3), 456 long range (i-j > or = 4) interresidue restraints and 207 non-trivial intraresidue restraints. 97 phi and 55 chi 1 angular restraints were also included in the calculation of a family of 20 structures using a combined distance geometry-simulated annealing protocol. Most regions of the protein are well defined in the calculations, with an RMSD of 0.525 A for backbone atoms excluding the metal binding loop (residues 34-48) and the last three C-terminal residues (residues 103-106). Where comparison is possible, these regions show an increase in dynamic behavior over the native protein, as does the loop containing residues 74-76. Structural and dynamic differences between native Pdx and GaPdx are discussed in relation to charge and packing of the metal binding site. The solution structure of a gallium-substituted putidaredoxin mutant: GaPdx C85S.,Pochapsky TC, Kuti M, Kazanis S J Biomol NMR. 1998 Oct;12(3):407-15. PMID:9835048[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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