View source for 4xou


==Crystal structure of the SR Ca2+-ATPase in the Ca2-E1-MgAMPPCP form determined by serial femtosecond crystallography using an X-ray free-electron laser.==
<StructureSection load='4xou' size='340' side='right' caption='[[4xou]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4xou]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XOU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XOU FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3n8g|3n8g]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Calcium-transporting_ATPase Calcium-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.8 3.6.3.8] </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=4xou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xou OCA], [http://pdbe.org/4xou PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xou RCSB], [http://www.ebi.ac.uk/pdbsum/4xou PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xou ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/AT2A1_RABIT AT2A1_RABIT]] This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction (By similarity). 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Membrane proteins are key players in biological systems, mediating signalling events and the specific transport of e.g. ions and metabolites. Consequently, membrane proteins are targeted by a large number of currently approved drugs. Understanding their functions and molecular mechanisms is greatly dependent on structural information, not least on complexes with functionally or medically important ligands. Structure determination, however, is hampered by the difficulty of obtaining well diffracting, macroscopic crystals. Here, the feasibility of X-ray free-electron-laser-based serial femtosecond crystallography (SFX) for the structure determination of membrane protein-ligand complexes using microcrystals of various native-source and recombinant P-type ATPase complexes is demonstrated. The data reveal the binding sites of a variety of ligands, including lipids and inhibitors such as the hallmark P-type ATPase inhibitor orthovanadate. By analyzing the resolution dependence of ligand densities and overall model qualities, SFX data quality metrics as well as suitable refinement procedures are discussed. Even at relatively low resolution and multiplicity, the identification of ligands can be demonstrated. This makes SFX a useful tool for ligand screening and thus for unravelling the molecular mechanisms of biologically active proteins.

Structural studies of P-type ATPase-ligand complexes using an X-ray free-electron laser.,Bublitz M, Nass K, Drachmann ND, Markvardsen AJ, Gutmann MJ, Barends TR, Mattle D, Shoeman RL, Doak RB, Boutet S, Messerschmidt M, Seibert MM, Williams GJ, Foucar L, Reinhard L, Sitsel O, Gregersen JL, Clausen JD, Boesen T, Gotfryd K, Wang KT, Olesen C, Moller JV, Nissen P, Schlichting I IUCrJ. 2015 Jun 11;2(Pt 4):409-20. doi: 10.1107/S2052252515008969. eCollection, 2015 Jul 1. PMID:26175901<ref>PMID:26175901</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4xou" style="background-color:#fffaf0;"></div>

==See Also==
*[[ATPase|ATPase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Calcium-transporting ATPase]]
[[Category: Oryctolagus cuniculus]]
[[Category: Barends, T R.M]]
[[Category: Boesen, T]]
[[Category: Boutet, S]]
[[Category: Bublitz, M]]
[[Category: Clausen, J D]]
[[Category: Doak, R B]]
[[Category: Drachmann, N D]]
[[Category: Foucar, L]]
[[Category: Gotfryd, K]]
[[Category: Gregersen, J L]]
[[Category: Gutmann, M J]]
[[Category: Markvardsen, A J]]
[[Category: Mattle, D]]
[[Category: Messerschmidt, M]]
[[Category: Moller, J V]]
[[Category: Nass, K]]
[[Category: Nissen, P]]
[[Category: Olesen, C]]
[[Category: Reinhard, L]]
[[Category: Schlichting, I]]
[[Category: Seibert, M M]]
[[Category: Shoeman, R L]]
[[Category: Sitsel, O]]
[[Category: Wang, K T]]
[[Category: Williams, G J]]
[[Category: Hydrolase]]
[[Category: P-type atpase]]
[[Category: Serial femtosecond crystallography]]
[[Category: X-ray free electron laser]]