3wdn
From Proteopedia
(Difference between revisions)
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- | + | ==High-resolution X-ray crystal structure of bovine H-protein using a high-pressure cryocooling method== | |
- | + | <StructureSection load='3wdn' size='340' side='right' caption='[[3wdn]], [[Resolution|resolution]] 0.86Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[3wdn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WDN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WDN FirstGlance]. <br> | |
- | ==Function== | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GCSH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wdn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wdn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wdn RCSB], [http://www.ebi.ac.uk/pdbsum/3wdn PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
[[http://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. | [[http://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. | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Recently, many technical improvements in macromolecular X-ray crystallography have increased the number of structures deposited in the Protein Data Bank and improved the resolution limit of protein structures. Almost all high-resolution structures have been determined using a synchrotron radiation source in conjunction with cryocooling techniques, which are required in order to minimize radiation damage. However, optimization of cryoprotectant conditions is a time-consuming and difficult step. To overcome this problem, the high-pressure cryocooling method was developed (Kim et al., 2005) and successfully applied to many protein-structure analyses. In this report, using the high-pressure cryocooling method, the X-ray crystal structure of bovine H-protein was determined at 0.86 A resolution. Structural comparisons between high- and ambient-pressure cryocooled crystals at ultra-high resolution illustrate the versatility of this technique. This is the first ultra-high-resolution X-ray structure obtained using the high-pressure cryocooling method. | ||
- | + | High-resolution X-ray crystal structure of bovine H-protein using the high-pressure cryocooling method.,Higashiura A, Ohta K, Masaki M, Sato M, Inaka K, Tanaka H, Nakagawa A J Synchrotron Radiat. 2013 Nov;20(Pt 6):989-93. doi: 10.1107/S090904951302373X., Epub 2013 Oct 5. PMID:24121354<ref>PMID:24121354</ref> | |
- | + | ||
- | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
- | + | </div> | |
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Bovin]] | [[Category: Bovin]] | ||
- | [[Category: Higashiura, A | + | [[Category: Higashiura, A]] |
- | [[Category: Nakagawa, A | + | [[Category: Nakagawa, A]] |
[[Category: Antiparallel beta sheet]] | [[Category: Antiparallel beta sheet]] | ||
[[Category: Beta sandwich]] | [[Category: Beta sandwich]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] |
Revision as of 13:03, 25 December 2014
High-resolution X-ray crystal structure of bovine H-protein using a high-pressure cryocooling method
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