2rhh

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Current revision (09:22, 21 February 2024) (edit) (undo)
 
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<StructureSection load='2rhh' size='340' side='right'caption='[[2rhh]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='2rhh' size='340' side='right'caption='[[2rhh]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2rhh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RHH FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2rhh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RHH FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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]] 2.001&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2rhj|2rhj]], [[2rhl|2rhl]], [[2rho|2rho]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ftsZ ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Bacillus globigii" Migula 1900])</td></tr>
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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=2rhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rhh OCA], [https://pdbe.org/2rhh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rhh RCSB], [https://www.ebi.ac.uk/pdbsum/2rhh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rhh 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=2rhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rhh OCA], [https://pdbe.org/2rhh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rhh RCSB], [https://www.ebi.ac.uk/pdbsum/2rhh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rhh ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/FTSZ_BACSU FTSZ_BACSU]] Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.<ref>PMID:15317782</ref> <ref>PMID:16159787</ref>
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[https://www.uniprot.org/uniprot/FTSZ_BACSU FTSZ_BACSU] Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.<ref>PMID:15317782</ref> <ref>PMID:16159787</ref>
== 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=2rhh 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=2rhh ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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BACKGROUND: With the goal of improving yield and success rates of heterologous protein production for structural studies we have developed the database and algorithm software package Gene Composer. This freely available electronic tool facilitates the information-rich design of protein constructs and their engineered synthetic gene sequences, as detailed in the accompanying manuscript. RESULTS: In this report, we compare heterologous protein expression levels from native sequences to that of codon engineered synthetic gene constructs designed by Gene Composer. A test set of proteins including a human kinase (P38alpha), viral polymerase (HCV NS5B), and bacterial structural protein (FtsZ) were expressed in both E. coli and a cell-free wheat germ translation system. We also compare the protein expression levels in E. coli for a set of 11 different proteins with greatly varied G:C content and codon bias. CONCLUSION: The results consistently demonstrate that protein yields from codon engineered Gene Composer designs are as good as or better than those achieved from the synonymous native genes. Moreover, structure guided N- and C-terminal deletion constructs designed with the aid of Gene Composer can lead to greater success in gene to structure work as exemplified by the X-ray crystallographic structure determination of FtsZ from Bacillus subtilis. These results validate the Gene Composer algorithms, and suggest that using a combination of synthetic gene and protein construct engineering tools can improve the economics of gene to structure research.
 
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Combined protein construct and synthetic gene engineering for heterologous protein expression and crystallization using Gene Composer.,Raymond A, Lovell S, Lorimer D, Walchli J, Mixon M, Wallace E, Thompkins K, Archer K, Burgin A, Stewart L BMC Biotechnol. 2009 Apr 21;9:37. PMID:19383143<ref>PMID:19383143</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 2rhh" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus globigii migula 1900]]
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[[Category: Bacillus subtilis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: ATCG3D, Accelerated Technologies Center for Gene to 3D Structure]]
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[[Category: Burgin A]]
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[[Category: Burgin, A]]
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[[Category: Halloran Z]]
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[[Category: Halloran, Z]]
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[[Category: Hjerrild K]]
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[[Category: Hjerrild, K]]
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[[Category: Lovell S]]
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[[Category: Lovell, S]]
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[[Category: Sheridan D]]
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[[Category: Sheridan, D]]
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[[Category: Stewart L]]
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[[Category: Stewart, L]]
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[[Category: Accelerated technologies center for gene to 3d structure]]
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[[Category: Atcg3d]]
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[[Category: Cell cycle]]
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[[Category: Cell division protein]]
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[[Category: Gtp-binding]]
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[[Category: Gtpase]]
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[[Category: Polymerization]]
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[[Category: PSI, Protein structure initiative]]
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[[Category: Structural genomic]]
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[[Category: Tubulin homolog]]
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Current revision

Synthetic Gene Encoded Bacillus Subtilis FtsZ with Bound Sulfate Ion

PDB ID 2rhh

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