5dsm: Difference between revisions

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 <StructureSection load='5dsm' size='340' side='right' caption='[[5dsm]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5dsm]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DSM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DSM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5dsm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DSM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DSM FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dsr|5dsr]], [[5dsq|5dsq]], [[5dsp|5dsp]], [[5dso|5dso]], [[5dsn|5dsn]], [[5dsl|5dsl]], [[5dsk|5dsk]], [[5dsj|5dsj]], [[5dsi|5dsi]]</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] </span></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=5dsm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dsm OCA], [http://pdbe.org/5dsm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dsm RCSB], [http://www.ebi.ac.uk/pdbsum/5dsm PDBsum]</span></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=5dsm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dsm OCA], [http://pdbe.org/5dsm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dsm RCSB], [http://www.ebi.ac.uk/pdbsum/5dsm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dsm ProSAT]</span></td></tr>
 </table>
 == Disease ==
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 == Function ==
 [[http://www.uniprot.org/uniprot/CAH2_HUMAN CAH2_HUMAN]] Essential for bone resorption and osteoclast differentiation (By similarity). Reversible hydration of carbon dioxide. Can hydrate cyanamide to urea. Involved in the regulation of fluid secretion into the anterior chamber of the eye.<ref>PMID:10550681</ref> <ref>PMID:11831900</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Carbonic anhydrases are mostly zinc metalloenzymes that catalyze the reversible hydration/dehydration of CO2/HCO3 (-) Previously, the X-ray crystal structures of CO2-bound holo (zinc-bound) and apo (zinc-free) human carbonic anhydrase IIs (hCA IIs) were captured at high resolution. Here, we present sequential timeframe structures of holo- [T = 0 s (CO2-bound), 50 s, 3 min, 10 min, 25 min, and 1 h] and apo-hCA IIs [T = 0 s, 50 s, 3 min, and 10 min] during the "slow" release of CO2 Two active site waters, WDW (deep water) and WDW' (this study), replace the vacated space created on CO2 release, and another water, WI (intermediate water), is seen to translocate to the proton wire position W1. In addition, on the rim of the active site pocket, a water W2' (this study), in close proximity to residue His64 and W2, gradually exits the active site, whereas His64 concurrently rotates from pointing away ("out") to pointing toward ("in") active site rotameric conformation. This study provides for the first time, to our knowledge, structural "snapshots" of hCA II intermediate states during the formation of the His64-mediated proton wire that is induced as CO2 is released. Comparison of the holo- and apo-hCA II structures shows that the solvent network rearrangements require the presence of the zinc ion.
+Tracking solvent and protein movement during CO2 release in carbonic anhydrase II crystals.,Kim CU, Song H, Avvaru BS, Gruner SM, Park S, McKenna R Proc Natl Acad Sci U S A. 2016 May 10;113(19):5257-62. doi:, 10.1073/pnas.1520786113. Epub 2016 Apr 25. PMID:27114542<ref>PMID:27114542</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 5dsm" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Carbonic anhydrase|Carbonic anhydrase]]
 == References ==
 <references/>
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 </StructureSection>
 [[Category: Carbonate dehydratase]]
+[[Category: Human]]
 [[Category: Kim, C U]]
 [[Category: McKenna, R]]