1t5t

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Image:1t5t.gif

1t5t, resolution 2.90Å

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Structure of the (SR)Ca2+-ATPase Ca2-E1-ADP:AlF4- form

Overview

A tight coupling between adenosine triphosphate (ATP) hydrolysis and vectorial ion transport has to be maintained by ATP-consuming ion pumps. We report two crystal structures of Ca2+-bound sarco(endo)plasmic reticulum Ca2+-adenosine triphosphatase (SERCA) at 2.6 and 2.9 angstrom resolution in complex with (i) a nonhydrolyzable ATP analog [adenosine (beta-gamma methylene)-triphosphate] and (ii) adenosine diphosphate plus aluminum fluoride. SERCA reacts with ATP by an associative mechanism mediated by two Mg2+ ions to form an aspartyl-phosphorylated intermediate state (Ca2-E1 approximately P). The conformational changes that accompany the reaction with ATP pull the transmembrane helices 1 and 2 and close a cytosolic entrance for Ca2+, thereby preventing backflow before Ca2+ is released on the other side of the membrane.

About this Structure

1T5T is a Single protein structure of sequence from Oryctolagus cuniculus with , , , and as ligands. Active as Calcium-transporting ATPase, with EC number 3.6.3.8 Full crystallographic information is available from OCA.

Reference

Phosphoryl transfer and calcium ion occlusion in the calcium pump., Sorensen TL, Moller JV, Nissen P, Science. 2004 Jun 11;304(5677):1672-5. PMID:15192230

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