Talk:P-type ATPase

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based upon their ability to catalyze auto- (or self-) phosphorylation (hence P) of a key conserved aspartate residue within the pump and? their energy source, adenosine triphosphate (should be from; also in places aspartate is used, in other places aspartic acid, recommend always using one of these only to be consistent)

Structure - E.g. the catalytic alpha subunit of Na+/K+-ATPase consists? of two additional subunits, beta and gamma (try the Na+/K+-ATPase consists of the catalytic alpha subunit and two additional subunits, beta and gamma)

Membrane section - and the large subfamily of heavy metal pumps P1B) - unbalanced )

which between subfamilies ranges from 2 to 6 - if P1A ATPases only have 7 transmembrane helices there would only be 1 (plus the 6 core segments)

Phosphorylation (P) domain - canonical aspartic acid residue phosphorylated (in a conserved DKTGT motif; the 'D' is the one letter abbreviation of the amino acid aspartate) during the reaction cycle - it would be clearer to move (in a conserved...) before phosphorylated

Actuator (A) domain - and it is pivot? in transporting - unclear whether this should be pivotal or a pivot)

P1 ATPases - P1 ATPases (or Type I ATPases) consists? of the transition/heavy metal ATPases - delete s; & potassium is neither a transition nor heavy metal

P1B ATPases - In the Archaeoglobus fulgidus CopA (TC# 3.A.3.5.7? (earlier CopA was 3.A.3.5.30)

Structural and mechanistic details of copper-transporting P-type ATPase functionhave - add space

P2 ATPases - (specific for Na+,K+, H+ Ca2+, Mg2+ and phospholipids) - add space before K & , after H+; none of the subgroups list phospholipids (which are given for P4 not P2)

P2A ATPases - Crystal structures of Sarcoplasmic/endoplasmic reticulum ATP driven calcium pumps - sarcoplasmic should not be capitalized & add - between ATP & driven

This unwinding of M4 is recognized as a key structural feature of P-type ATPases - if this is the case for all P-type ATPases it should be mentioned at the beginning rather than here; if not change P-type to P2A

The Ca2E1~P state becomes formed - better if becomes is changed to is

This is in agreement with the general model form? substrate translocation (delete m)

is not used to bind the substrate but to release it again? from the buried counter ions

Xu et al. proposed how Ca2+ binding induces conformational changes in TMS 4 and 5 - it would be better to be consistent and use M4 & M5 (if that's correct)

The nucleotide binding (N) and b-sheet? (b) domains (is that the A domain; again, be consistent)

phosphoryl analogs BeF, AlF, MgF - there should be more than one F atom (& should that be phosphate instead?)

Crystal Structures of Calcium ATPase are available - don't capitalize structures & calcium

P2B ATPases - P2B (or type IIB ATPases) are - either add ATPases after P2B or move ) to after IIB

P2D ATPases - small number of Na+ (and K+) exporting - add - before exporting

P3B ATPases - Fungal H+ transporters (TC# 3.A.3.3) and Mg2+ (TC# 3.A.3.4) ? (sentence fragment)

Further phylogenetic classification - which as of early 2016 consisting? of 20 families (consisted)

In eukaryotes, they are present in the plasma membranes or endoplasmic reticular? (reticulum)

more extensive analysis of the P-type ATPase Superfamily in Prokaryotes and compared them with those from Eukaryotes - don't capitalize superfamily, prokaryotes, or eukaryotes

others are found only in one of? the other type (try or)

Horizontal gene transfer - (e.g. Kdp-type K+ uptake ATPases (type III?) - & add - after K+

Human genes - P2A: secretory - ATP2C2 is given twice

    108.18.223.247 (talk) 09:07, 16 November 2020 (UTC)[reply]