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1plc

From Proteopedia

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[[Image:1plc.gif|left|200px]]
 
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{{Structure
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==ACCURACY AND PRECISION IN PROTEIN CRYSTAL STRUCTURE ANALYSIS: RESTRAINED LEAST-SQUARES REFINEMENT OF THE CRYSTAL STRUCTURE OF POPLAR PLASTOCYANIN AT 1.33 ANGSTROMS RESOLUTION==
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|PDB= 1plc |SIZE=350|CAPTION= <scene name='initialview01'>1plc</scene>, resolution 1.33&Aring;
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<StructureSection load='1plc' size='340' side='right'caption='[[1plc]], [[Resolution|resolution]] 1.33&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CU:COPPER (II) ION'>CU</scene>
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<table><tr><td colspan='2'>[[1plc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Populus_nigra Populus nigra]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1pcy 1pcy]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PLC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PLC FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.33&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>
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}}
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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=1plc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1plc OCA], [https://pdbe.org/1plc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1plc RCSB], [https://www.ebi.ac.uk/pdbsum/1plc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1plc ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PLAS1_POPNI PLAS1_POPNI] Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pl/1plc_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1plc ConSurf].
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<div style="clear:both"></div>
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'''ACCURACY AND PRECISION IN PROTEIN CRYSTAL STRUCTURE ANALYSIS: RESTRAINED LEAST-SQUARES REFINEMENT OF THE CRYSTAL STRUCTURE OF POPLAR PLASTOCYANIN AT 1.33 ANGSTROMS RESOLUTION'''
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==See Also==
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*[[Plastocyanin 3D structures|Plastocyanin 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The structure of the electron-transfer protein, plastocyanin (99 amino acids, one Cu atom, 10,500 Da) from poplar leaves, has been refined at 1.33 A resolution to a residual R = 0.15. The space group is orthorhombic, P2(1)2(1)2(1), a = 29.60 (1), b = 46.86 (3), c = 57.60 (3) A. The 14,303 reflections used in the refinement were obtained from a data set recorded on a four-circle diffractometer with radiation from a sealed fine-focus tube, combined with a data set measured on oscillation films exposed at the DESY synchrotron. The final model comprises 1442 (738 non-H) protein atoms, one Cu atom and 110 solvent molecules. Nine residues are described as disordered. The root-mean-square deviation from ideal bond lengths is 0.016 A and the root-mean-square difference between the positions of the C alpha atoms in this refined model and in the structure previously refined at 1.6 A resolution is 0.11 A. The effects of manual model adjustment, resolution, choice of standard values for geometrical parameters, inclusion of H atoms and inclusion of anomalous-scattering corrections on the copper-site geometry have been explored. The final values of the Cu-ligand bond lengths are: Cu--N(His37) 1.91, Cu--S(Cys84) 2.07, Cu--N(His87) 2.06, Cu--S(Met92) 2.82 A.
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[[Category: Large Structures]]
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==About this Structure==
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1PLC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Populus_nigra Populus nigra]. This structure supersedes the now removed PDB entry 1PCY. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PLC OCA].
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==Reference==
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Accuracy and precision in protein structure analysis: restrained least-squares refinement of the structure of poplar plastocyanin at 1.33 A resolution., Guss JM, Bartunik HD, Freeman HC, Acta Crystallogr B. 1992 Dec 1;48 ( Pt 6):790-811. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1492962 1492962]
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[[Category: Populus nigra]]
[[Category: Populus nigra]]
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[[Category: Single protein]]
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[[Category: Freeman HC]]
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[[Category: Freeman, H C.]]
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[[Category: Guss JM]]
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[[Category: Guss, J M.]]
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[[Category: CU]]
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[[Category: electron transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:25:53 2008''
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Current revision

ACCURACY AND PRECISION IN PROTEIN CRYSTAL STRUCTURE ANALYSIS: RESTRAINED LEAST-SQUARES REFINEMENT OF THE CRYSTAL STRUCTURE OF POPLAR PLASTOCYANIN AT 1.33 ANGSTROMS RESOLUTION

PDB ID 1plc

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