View source for 3klr


==Bovine H-protein at 0.88 angstrom resolution==
<StructureSection load='3klr' size='340' side='right'caption='[[3klr]], [[Resolution|resolution]] 0.88&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3klr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KLR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KLR FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.88&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3klr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3klr OCA], [https://pdbe.org/3klr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3klr RCSB], [https://www.ebi.ac.uk/pdbsum/3klr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3klr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GCSH_BOVIN GCSH_BOVIN] The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
== 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/kl/3klr_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/main_output.php?pdb_ID=3klr ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Recent technical improvements in macromolecular X-ray crystallography have significantly improved the resolution limit of protein structures. However, examples of high-resolution structure determination are still limited. In this study, the X-ray crystal structure of bovine H-protein, a component of the glycine cleavage system, was determined at 0.88 A resolution. This is the first ultrahigh-resolution structure of an H-protein. The data were collected using synchrotron radiation. Because of limitations of the hardware, especially the dynamic range of the CCD detector, three data sets (high-, medium- and low-resolution data sets) were measured in order to obtain a complete set of data. To improve the quality of the merged data, the reference data set was optimized for merging and the merged data were assessed by comparing merging statistics and R factors against the final model and the number of visualized H atoms. In addition, the advantages of merging three data sets were evaluated. The omission of low-resolution reflections had an adverse effect on visualization of H atoms in hydrogen-omit maps. Visualization of hydrogen electron density is a good indicator for assessing the quality of high-resolution X-ray diffraction data.

High-resolution X-ray crystal structure of bovine H-protein at 0.88 A resolution.,Higashiura A, Kurakane T, Matsuda M, Suzuki M, Inaka K, Sato M, Kobayashi T, Tanaka T, Tanaka H, Fujiwara K, Nakagawa A Acta Crystallogr D Biol Crystallogr. 2010 Jun;66(Pt 6):698-708. Epub 2010 May 15. PMID:20516622<ref>PMID:20516622</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3klr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Fujiwara K]]
[[Category: Higashiura A]]
[[Category: Inaka K]]
[[Category: Kurakane T]]
[[Category: Matsuda M]]
[[Category: Nakagawa A]]
[[Category: Sato M]]
[[Category: Suzuki M]]
[[Category: Tanaka H]]