2hxx: Difference between revisions

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{{Seed}}
[[Image:2hxx.png|left|200px]]


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==Aminotryptophan Barstar==
The line below this paragraph, containing "STRUCTURE_2hxx", creates the "Structure Box" on the page.
<StructureSection load='2hxx' size='340' side='right'caption='[[2hxx]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2hxx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HXX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HXX FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</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&#8491;</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=4IN:4-AMINO-L-TRYPTOPHAN'>4IN</scene></td></tr>
{{STRUCTURE_2hxx|  PDB=2hxx  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hxx OCA], [https://pdbe.org/2hxx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hxx RCSB], [https://www.ebi.ac.uk/pdbsum/2hxx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hxx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BARS_BACAM BARS_BACAM] Inhibitor of the ribonuclease barnase. Forms a one-to-one non-covalent complex.
== 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/hx/2hxx_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=2hxx ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The indole ring of the canonical amino acid tryptophan (Trp) possesses distinguished features, such as sterical bulk, hydrophobicity and the nitrogen atom which is capable of acting as a hydrogen bond donor. The introduction of an amino group into the indole moiety of Trp yields the structural analogs 4-aminotryptophan ((4-NH(2))Trp) and 5-aminotryptophan ((5-NH(2))Trp). Their hydrophobicity and spectral properties are substantially different when compared to those of Trp. They resemble the purine bases of DNA and share their capacity for pH-sensitive intramolecular charge transfer. The Trp --&gt; aminotryptophan substitution in proteins during ribosomal translation is expected to result in related protein variants that acquire these features. These expectations have been fulfilled by incorporating (4-NH(2))Trp and (5-NH(2))Trp into barstar, an intracellular inhibitor of the ribonuclease barnase from Bacillus amyloliquefaciens. The crystal structure of (4-NH(2))Trp-barstar is similar to that of the parent protein, whereas its spectral and thermodynamic behavior is found to be remarkably different. The T(m) value of (4-NH(2))Trp- and (5-NH(2))Trp-barstar is lowered by about 20 degrees Celsius, and they exhibit a strongly reduced unfolding cooperativity and substantial loss of free energy in folding. Furthermore, folding kinetic study of (4-NH(2))Trp-barstar revealed that the denatured state is even preferred over native one. The combination of structural and thermodynamic analyses clearly shows how structures of substituted barstar display a typical structure-function tradeoff: the acquirement of unique pH-sensitive charge transfer as a novel function is achieved at the expense of protein stability. These findings provide a new insight into the evolution of the amino acid repertoire of the universal genetic code and highlight possible problems regarding protein engineering and design by using an expanded genetic code.


===Aminotryptophan Barstar===
Aminotryptophan-containing barstar: structure--function tradeoff in protein design and engineering with an expanded genetic code.,Rubini M, Lepthien S, Golbik R, Budisa N Biochim Biophys Acta. 2006 Jul;1764(7):1147-58. Epub 2006 May 10. PMID:16782415<ref>PMID:16782415</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2hxx" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_16782415}}, adds the Publication Abstract to the page
*[[Barstar 3D structures|Barstar 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 16782415 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_16782415}}
__TOC__
 
</StructureSection>
==About this Structure==
2HXX is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HXX OCA].
 
==Reference==
<ref group="xtra">PMID:16782415</ref><references group="xtra"/>
[[Category: Bacillus amyloliquefaciens]]
[[Category: Bacillus amyloliquefaciens]]
[[Category: Budisa, N.]]
[[Category: Large Structures]]
[[Category: Golbik, R.]]
[[Category: Budisa N]]
[[Category: Lepthien, S.]]
[[Category: Golbik R]]
[[Category: Rubini, M.]]
[[Category: Lepthien S]]
[[Category: Aminotryptophan]]
[[Category: Rubini M]]
[[Category: Barstar]]
[[Category: Genetic code]]
[[Category: Protein folding]]
[[Category: Stability]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 13:40:41 2009''
Retrieved from "https://proteopedia.org/2hxx"