GHKL domain

{{Short description|Evolutionary conserved protein domain}}

{{Infobox protein family

| Symbol = HATPase_c

| Name = Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase

| image = PDB 1ah6 EBI.jpg

| width =

| caption = Structure of the N-terminal domain of the yeast Hsp90 chaperone.{{cite journal |vauthors=Prodromou C, Roe SM, Piper PW, Pearl LH |title=A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone |journal=Nat. Struct. Biol. |volume=4 |issue=6 |pages=477–82 |date=June 1997 |pmid=9187656 |doi= 10.1038/nsb0697-477|s2cid=38764610 }}

| Pfam= PF02518

| InterPro= IPR003594

| SMART= HATPase_c

| Prosite =

| SCOP = 1ei1

| TCDB =

| OPM family=

| OPM protein=

| CDD = cd00075

| PDB=

{{PDB3|1ys3}}B:338-445 {{PDB3|1ysr}}B:338-445 {{PDB3|1id0}}A:374-479

{{PDB3|2c2a}}A:365-479 {{PDB3|1i58}}A:398-540 {{PDB3|1b3q}}B:398-540

{{PDB3|1i5b}}A:398-540 {{PDB3|1i5a}}B:398-540 {{PDB3|1i5d}}A:398-540

{{PDB3|1i5c}}B:398-540 {{PDB3|1i59}}B:398-540 {{PDB3|1y8n}}A:236-361

{{PDB3|1y8o}}A:236-361 {{PDB3|1y8p}}A:236-361 {{PDB3|1jm6}}A:240-363

{{PDB3|1gkx}}A:264-403 {{PDB3|1gkz}}A:264-403 {{PDB3|1gjv}}A:264-403

{{PDB3|1nhj}}A:18-79 {{PDB3|1nhi}}A:18-79 {{PDB3|1nhh}}A:18-79

{{PDB3|1b62}}A:18-79 {{PDB3|1bkn}}B:20-73 {{PDB3|1b63}}A:18-79

{{PDB3|1h7s}}A:30-164 {{PDB3|1h7u}}A:30-164 {{PDB3|1ea6}}B:30-164

{{PDB3|1mx0}}D:27-179 {{PDB3|1mu5}}A:27-179 {{PDB3|1z5b}}A:27-179

{{PDB3|1z5c}}B:27-179 {{PDB3|1z59}}A:27-179 {{PDB3|1z5a}}B:27-179

{{PDB3|1thn}}C:35-136 {{PDB3|1tid}}C:35-136 {{PDB3|1l0o}}A:35-136

{{PDB3|1til}}E:35-136 {{PDB3|1th8}}A:35-136 {{PDB3|1ah6}} :26-180

{{PDB3|1us7}}A:26-180 {{PDB3|1amw}} :26-180 {{PDB3|2bre}}A:26-180

{{PDB3|2akp}}B:26-180 {{PDB3|1a4h}} :26-180 {{PDB3|1ah8}}A:26-180

{{PDB3|2brc}}A:26-180 {{PDB3|1am1}} :26-180 {{PDB3|1bgq}}A:26-180

{{PDB3|1yc4}}A:40-193 {{PDB3|1uyg}}A:40-193 {{PDB3|2bt0}}A:40-193

{{PDB3|1uyc}}A:40-193 {{PDB3|1yer}} :40-193 {{PDB3|1yc3}}A:40-193

{{PDB3|1uy8}}A:40-193 {{PDB3|2bz5}}A:40-193 {{PDB3|1uye}}A:40-193

{{PDB3|2byh}}A:40-193 {{PDB3|1yc1}}A:40-193 {{PDB3|1uyh}}A:40-193

{{PDB3|1uy9}}A:40-193 {{PDB3|1uyd}}A:40-193 {{PDB3|1uy6}}A:40-193

{{PDB3|1uy7}}A:40-193 {{PDB3|2bsm}}A:40-193 {{PDB3|1yes}} :40-193

{{PDB3|1uyl}}A:40-193 {{PDB3|1uyi}}A:40-193 {{PDB3|2byi}}A:40-193

{{PDB3|1uyf}}A:40-193 {{PDB3|1byq}}A:40-193 {{PDB3|1uyk}}A:40-193

{{PDB3|1osf}}A:40-193 {{PDB3|1yet}} :40-193 {{PDB3|1uym}}A:35-188

{{PDB3|1tc0}}B:96-254 {{PDB3|1ysz}}A:96-254 {{PDB3|1u2o}}B:96-254

{{PDB3|1yt0}}A:96-254 {{PDB3|1tbw}}A:96-254 {{PDB3|1qye}}A:96-254

{{PDB3|1u0z}}A:96-254 {{PDB3|1yt2}}A:96-254 {{PDB3|1tc6}}A:96-254

{{PDB3|1u0y}}A:96-254 {{PDB3|1qy8}}A:96-254 {{PDB3|1yt1}}A:96-254

{{PDB3|1qy5}}A:96-254 {{PDB3|1y4u}}B:27-183 {{PDB3|1y4s}}A:27-183

{{PDB3|1kij}}A:28-173 {{PDB3|1s16}}A:27-172 {{PDB3|1s14}}B:27-172

{{PDB3|1pvg}}A:55-204 {{PDB3|1qzr}}B:55-204 {{PDB3|1zxn}}C:76-224

{{PDB3|1zxm}}A:76-224

}}

The GHKL domain (Gyrase, Hsp90, Histidine Kinase, MutL) is an evolutionary conserved protein domain.{{cite journal |vauthors=Dutta R, Inouye M |title=GHKL, an emergent ATPase/kinase superfamily |journal=Trends Biochem. Sci. |volume=25 |issue=1 |pages=24–8 |date=January 2000 |pmid=10637609 |doi= 10.1016/S0968-0004(99)01503-0}} It is an ATPase domain found in several ATP-binding proteins such as histidine kinase, DNA gyrase B, topoisomerases,{{cite journal |vauthors=Bellon S, Parsons JD, Wei Y, Hayakawa K, Swenson LL, Charifson PS, Lippke JA, Aldape R, Gross CH | title = Crystal Structures of Escherichia coli Topoisomerase IV ParE Subunit (24 and 43 Kilodaltons): a Single Residue Dictates Differences in Novobiocin Potency against Topoisomerase IV and DNA Gyrase | journal = Antimicrob. Agents Chemother. | volume = 48 | issue = 5 | pages = 1856–64 |date=May 2004 | pmid = 15105144 | pmc = 400558 | doi = 10.1128/AAC.48.5.1856-1864.2004}} heat shock protein HSP90,{{cite journal |vauthors=Immormino RM, Dollins DE, Shaffer PL, Soldano KL, Walker MA, Gewirth DT | title = Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone | journal = J. Biol. Chem. | volume = 279 | issue = 44 | pages = 46162–71 |date=October 2004 | pmid = 15292259 | doi = 10.1074/jbc.M405253200 | doi-access = free }}{{cite journal |vauthors=Roe SM, Ali MM, Meyer P, Vaughan CK, Panaretou B, Piper PW, Prodromou C, Pearl LH | title = The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37) | journal = Cell | volume = 116 | issue = 1 | pages = 87–98 |date=January 2004 | pmid = 14718169 | doi = 10.1016/S0092-8674(03)01027-4| s2cid = 797232 | doi-access = free }}{{cite journal |vauthors=Wright L, Barril X, Dymock B, Sheridan L, Surgenor A, Beswick M, Drysdale M, Collier A, Massey A, Davies N, Fink A, Fromont C, Aherne W, Boxall K, Sharp S, Workman P, Hubbard RE | title = Structure-activity relationships in purine-based inhibitor binding to HSP90 isoforms | journal = Chem. Biol. | volume = 11 | issue = 6 | pages = 775–85 |date=June 2004 | pmid = 15217611 | doi = 10.1016/j.chembiol.2004.03.033 | doi-access = free }} phytochrome-like ATPases and DNA mismatch repair proteins.

More information about this protein can be found at Protein of the Month: DNA Topoisomerase.{{cite web | url = http://www.ebi.ac.uk/interpro/potm/2006_1/Page1.htm | title = DNA Topoisomerase | author = McDowall J | date = 2006 | work = Protein of the month | publisher = InterPro }}