1d03: Difference between revisions

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<StructureSection load='1d03' size='340' side='right'caption='[[1d03]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
<StructureSection load='1d03' size='340' side='right'caption='[[1d03]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1d03]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Anacystis_nidulans_r2 Anacystis nidulans r2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D03 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D03 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1d03]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus_PCC_7942_=_FACHB-805 Synechococcus elongatus PCC 7942 = FACHB-805]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D03 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D03 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1czn|1czn]], [[1czu|1czu]], [[1czl|1czl]], [[1d04|1d04]], [[1czh|1czh]], [[1czo|1czo]], [[1czr|1czr]], [[1czk|1czk]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></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=1d03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d03 OCA], [https://pdbe.org/1d03 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d03 RCSB], [https://www.ebi.ac.uk/pdbsum/1d03 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d03 ProSAT]</span></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=1d03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d03 OCA], [https://pdbe.org/1d03 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d03 RCSB], [https://www.ebi.ac.uk/pdbsum/1d03 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d03 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/FLAV_SYNE7 FLAV_SYNE7]] Low-potential electron donor to a number of redox enzymes.  
[https://www.uniprot.org/uniprot/FLAV_SYNE7 FLAV_SYNE7] Low-potential electron donor to a number of redox enzymes.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1d03 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=1d03 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Flavodoxin from Anacystis nidulans (Synechococcus PCC 7942) was the first member of the flavodoxin family to be characterized, and is the structural prototype for the "long-chain" flavodoxins that have molecular masses of approximately 20 kDa. Crystal structure analyses and refinements of three orthorhombic forms of oxidized A. nidulans flavodoxin are reported, and salient features of the fold and the FMN binding site are compared with other flavodoxins. The structure of form I (wild-type: P212121, a=57.08 A, b=69.24 A, c=45.55 A), determined initially by multiple isomorphous replacement, has been refined to R=0.183 and R(free)=0.211 for data from 10.0 to 1.7 A resolution. Structures of form II (wild-type: P212121, a=60.05 A, b=65.85 A, c=51.36 A) and form III (Asn58Gly: P212121, a=51.30 A, b=59.15 A, c=94.44 A) have been determined by molecular replacement and refined versus data to 2.0 A and 1.85 A, respectively; the R values for forms II and III are 0.147 and 0.150. Changes in the molecular contacts that produce the alternative packings in these crystalline forms are analyzed. Deletion of the Asn side-chain in the mutant Asn58Gly removes an intermolecular stacking interaction and allows the alternative packing found in form III crystals. The functionally important 50's loop of the FMN binding site is less restrained by intermolecular contacts in these crystals but maintains the same conformation as in oxidized wild type protein. The structures reported here provide the starting point for structure-function studies of the reduced states and of mutants, described in the accompanying paper.
Refined structures of oxidized flavodoxin from Anacystis nidulans.,Drennan CL, Pattridge KA, Weber CH, Metzger AL, Hoover DM, Ludwig ML J Mol Biol. 1999 Dec 3;294(3):711-24. PMID:10610791<ref>PMID:10610791</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1d03" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Flavodoxin 3D structures|Flavodoxin 3D structures]]
*[[Flavodoxin 3D structures|Flavodoxin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Anacystis nidulans r2]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Drennan, C L]]
[[Category: Synechococcus elongatus PCC 7942 = FACHB-805]]
[[Category: Hoover, D M]]
[[Category: Drennan CL]]
[[Category: Ludwig, M L]]
[[Category: Hoover DM]]
[[Category: Metzger, A L]]
[[Category: Ludwig ML]]
[[Category: Pattridge, K A]]
[[Category: Metzger AL]]
[[Category: Weber, C H]]
[[Category: Pattridge KA]]
[[Category: Electron transport]]
[[Category: Weber CH]]
[[Category: Flavodoxin]]
[[Category: Fmn binding]]
[[Category: Redox potential]]

Latest revision as of 09:47, 7 February 2024

REFINED STRUCTURES OF OXIDIZED FLAVODOXIN FROM ANACYSTIS NIDULANSREFINED STRUCTURES OF OXIDIZED FLAVODOXIN FROM ANACYSTIS NIDULANS

Structural highlights

1d03 is a 1 chain structure with sequence from Synechococcus elongatus PCC 7942 = FACHB-805. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.85Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FLAV_SYNE7 Low-potential electron donor to a number of redox enzymes.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1d03, resolution 1.85Å

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