2oa0: Difference between revisions
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New page: left|200px<br /><applet load="2oa0" size="450" color="white" frame="true" align="right" spinBox="true" caption="2oa0, resolution 3.400Å" /> '''Crystal structure o... |
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[[Image:2oa0.gif|left|200px]]<br /><applet load="2oa0" size=" | [[Image:2oa0.gif|left|200px]]<br /><applet load="2oa0" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2oa0, resolution 3.400Å" /> | caption="2oa0, resolution 3.400Å" /> | ||
'''Crystal structure of Calcium ATPase with bound ADP and cyclopiazonic acid'''<br /> | '''Crystal structure of Calcium ATPase with bound ADP and cyclopiazonic acid'''<br /> | ||
==Overview== | ==Overview== | ||
The sarcoplasmic reticulum Ca(2+)-ATPase is essential for calcium reuptake | The sarcoplasmic reticulum Ca(2+)-ATPase is essential for calcium reuptake in the muscle contraction-relaxation cycle. Here we present structures of a calcium-free state with bound cyclopiazonic acid (CPA) and magnesium fluoride at 2.65 A resolution and a calcium-free state with bound CPA and ADP at 3.4A resolution. In both structures, CPA occupies the calcium access channel delimited by transmembrane segments M1-M4. Inhibition of Ca(2+)-ATPase is stabilized by a polar pocket that surrounds the tetramic acid of CPA and a hydrophobic platform that cradles the inhibitor. The calcium pump residues involved include Gln(56), Leu(61), Val(62), and Asn(101). We conclude that CPA inhibits the calcium pump by blocking the calcium access channel and immobilizing a subset of transmembrane helices. In the E2(CPA) structure, ADP is bound in a distinct orientation within the nucleotide binding pocket. The adenine ring is sandwiched between Arg(489) of the nucleotide-binding domain and Arg(678) of the phosphorylation domain. This mode of binding conforms to an adenine recognition motif commonly found in ATP-dependent proteins. | ||
==About this Structure== | ==About this Structure== | ||
2OA0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with MG, CZA and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | 2OA0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CZA:'>CZA</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OA0 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Moncoq, K | [[Category: Moncoq, K A.]] | ||
[[Category: Young, H | [[Category: Young, H S.]] | ||
[[Category: ADP]] | [[Category: ADP]] | ||
[[Category: CZA]] | [[Category: CZA]] | ||
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[[Category: x-ray crystallography]] | [[Category: x-ray crystallography]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:16:06 2008'' | ||
