The structure of Mg-ATPase nucleotide-binding domain at 1.6 Å resolution reveals a unique ATP-binding motif
The structure of the nucleotide‐binding domain of the Mg‐ATPase MgtA from Escherichia coli has been solved and refined to 1.6 Å resolution. The structure is made up of a six‐stranded β‐sheet and a bundle of three α‐helices, with the nucleotide‐binding site sandwiched in between. The MgtA nucleotide‐...
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| Veröffentlicht in: | Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2009-11, Vol.65 (11), p.1181-1186 |
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| container_issue | 11 |
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| container_title | Acta crystallographica. Section D, Biological crystallography. |
| container_volume | 65 |
| creator | Håkansson, Kjell O. |
| description | The structure of the nucleotide‐binding domain of the Mg‐ATPase MgtA from Escherichia coli has been solved and refined to 1.6 Å resolution. The structure is made up of a six‐stranded β‐sheet and a bundle of three α‐helices, with the nucleotide‐binding site sandwiched in between. The MgtA nucleotide‐binding domain is shorter and more compact compared with that of the related Ca‐ATPase and lacks one of the β‐strands at the edge of the β‐sheet. The ATP‐binding pocket is surrounded by three sequence and structural motifs known from other P‐type ATPases and a fourth unique motif that is found only in Mg‐ATPases. This motif consists of a short polypeptide stretch running very close to the ATP‐binding site, while in Ca‐ATPase the binding site is more open, with the corresponding polypeptide segment folded away from the active site. |
| doi_str_mv | 10.1107/S090744490903306X |
| format | Article |
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Section D, Biological crystallography.</title><addtitle>Acta Cryst. D</addtitle><description>The structure of the nucleotide‐binding domain of the Mg‐ATPase MgtA from Escherichia coli has been solved and refined to 1.6 Å resolution. The structure is made up of a six‐stranded β‐sheet and a bundle of three α‐helices, with the nucleotide‐binding site sandwiched in between. The MgtA nucleotide‐binding domain is shorter and more compact compared with that of the related Ca‐ATPase and lacks one of the β‐strands at the edge of the β‐sheet. The ATP‐binding pocket is surrounded by three sequence and structural motifs known from other P‐type ATPases and a fourth unique motif that is found only in Mg‐ATPases. This motif consists of a short polypeptide stretch running very close to the ATP‐binding site, while in Ca‐ATPase the binding site is more open, with the corresponding polypeptide segment folded away from the active site.</description><subject>Adenosine Triphosphatases - chemistry</subject><subject>Adenosine Triphosphatases - metabolism</subject><subject>Adenosine Triphosphate - chemistry</subject><subject>Adenosine Triphosphate - metabolism</subject><subject>Amino Acid Sequence</subject><subject>ATP binding</subject><subject>Binding Sites</subject><subject>Crystallography, X-Ray</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>membrane proteins</subject><subject>Membrane Transport Proteins - chemistry</subject><subject>Membrane Transport Proteins - metabolism</subject><subject>MgtA</subject><subject>MgtB</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>P-type ATPases</subject><subject>Protein Binding</subject><subject>Protein Folding</subject><subject>Protein Interaction Domains and Motifs</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><issn>1399-0047</issn><issn>0907-4449</issn><issn>1399-0047</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkM1OFEEUhStEA4g8gBtTO1eNt7qq62c5GXE04mjCAOqmUt19G0v7B6u6VXZseDLexCehyEzAxIWrexbfd3JzCHnG4IAxUC-PwYASQph0OQf5aYvsMm5MBiDUo7_yDnkS4zcAyHOutskOMyYFxndJv_qKNI5hqsYpIB0a-v48m60-uoi0n6oWh9HXmJW-r31_Tuuhc76nbqTsQP65ur65pgHj0E6jH_oUf6JrI3V06v2PCWkqule71NQ8JY-bROD-5u6Rk9eHq_mb7OjD4u18dpRVHHKdMVkWTjZ1XjBXaJajBNRaO25YLfO6kKooQeeoKqGBCydKbkQNrDSFaxot-B55se69CEN6JI6287HCtnU9DlO0igsmFEiTSLYmqzDEGLCxF8F3LlxaBvZuZfvPysl5vmmfyg7rB2MzawL0GvjlW7z8f6OdfX51uCy40knN1qqPI_6-V134bqXiqrBny4UVy_lpbhbv7Bd-C7_llzU</recordid><startdate>200911</startdate><enddate>200911</enddate><creator>Håkansson, Kjell O.</creator><general>International Union of Crystallography</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>200911</creationdate><title>The structure of Mg-ATPase nucleotide-binding domain at 1.6 Å resolution reveals a unique ATP-binding motif</title><author>Håkansson, Kjell O.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3028-16b5a6fd251a5812e60e888a391d62d5675b082e7c48034a4b394d01b95aff843</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Adenosine Triphosphatases - chemistry</topic><topic>Adenosine Triphosphatases - metabolism</topic><topic>Adenosine Triphosphate - chemistry</topic><topic>Adenosine Triphosphate - metabolism</topic><topic>Amino Acid Sequence</topic><topic>ATP binding</topic><topic>Binding Sites</topic><topic>Crystallography, X-Ray</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli Proteins - chemistry</topic><topic>Escherichia coli Proteins - metabolism</topic><topic>membrane proteins</topic><topic>Membrane Transport Proteins - chemistry</topic><topic>Membrane Transport Proteins - metabolism</topic><topic>MgtA</topic><topic>MgtB</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>P-type ATPases</topic><topic>Protein Binding</topic><topic>Protein Folding</topic><topic>Protein Interaction Domains and Motifs</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Håkansson, Kjell O.</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Acta crystallographica. Section D, Biological crystallography.</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Håkansson, Kjell O.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The structure of Mg-ATPase nucleotide-binding domain at 1.6 Å resolution reveals a unique ATP-binding motif</atitle><jtitle>Acta crystallographica. Section D, Biological crystallography.</jtitle><addtitle>Acta Cryst. D</addtitle><date>2009-11</date><risdate>2009</risdate><volume>65</volume><issue>11</issue><spage>1181</spage><epage>1186</epage><pages>1181-1186</pages><issn>1399-0047</issn><issn>0907-4449</issn><eissn>1399-0047</eissn><abstract>The structure of the nucleotide‐binding domain of the Mg‐ATPase MgtA from Escherichia coli has been solved and refined to 1.6 Å resolution. The structure is made up of a six‐stranded β‐sheet and a bundle of three α‐helices, with the nucleotide‐binding site sandwiched in between. The MgtA nucleotide‐binding domain is shorter and more compact compared with that of the related Ca‐ATPase and lacks one of the β‐strands at the edge of the β‐sheet. The ATP‐binding pocket is surrounded by three sequence and structural motifs known from other P‐type ATPases and a fourth unique motif that is found only in Mg‐ATPases. This motif consists of a short polypeptide stretch running very close to the ATP‐binding site, while in Ca‐ATPase the binding site is more open, with the corresponding polypeptide segment folded away from the active site.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>International Union of Crystallography</pub><pmid>19923713</pmid><doi>10.1107/S090744490903306X</doi><tpages>6</tpages></addata></record> |
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| ispartof | Acta crystallographica. Section D, Biological crystallography., 2009-11, Vol.65 (11), p.1181-1186 |
| issn | 1399-0047 0907-4449 1399-0047 |
| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Alma/SFX Local Collection |
| subjects | Adenosine Triphosphatases - chemistry Adenosine Triphosphatases - metabolism Adenosine Triphosphate - chemistry Adenosine Triphosphate - metabolism Amino Acid Sequence ATP binding Binding Sites Crystallography, X-Ray Escherichia coli - enzymology Escherichia coli Proteins - chemistry Escherichia coli Proteins - metabolism membrane proteins Membrane Transport Proteins - chemistry Membrane Transport Proteins - metabolism MgtA MgtB Models, Molecular Molecular Sequence Data P-type ATPases Protein Binding Protein Folding Protein Interaction Domains and Motifs Sequence Alignment Sequence Homology, Amino Acid |
| title | The structure of Mg-ATPase nucleotide-binding domain at 1.6 Å resolution reveals a unique ATP-binding motif |
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