Crystallization and preliminary X-ray diffraction analysis of a soluble domain of the putative zinc transporter CzrB from Thermus thermophilus
CzrB is a putative zinc transporter from Thermus thermophilus. The protein is proposed to consist of a hexahelical transmembrane domain with a cytosolic extramembranal C‐terminus. The latter 92‐residue fragment may be expressed free and may function independently of the full‐length integral membrane...
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| Veröffentlicht in: | Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2007-08, Vol.63 (8), p.673-677 |
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| container_title | Acta crystallographica. Section F, Structural biology and crystallization communications |
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| creator | Höfer, Nicole Kolaj, Olga Li, Hui Cherezov, Vadim Gillilan, Richard Wall, J. Gerard Caffrey, Martin |
| description | CzrB is a putative zinc transporter from Thermus thermophilus. The protein is proposed to consist of a hexahelical transmembrane domain with a cytosolic extramembranal C‐terminus. The latter 92‐residue fragment may be expressed free and may function independently of the full‐length integral membrane protein. A 6×His‐tagged form of the water‐soluble fragment has been overexpressed in Escherichia coli and diffraction‐quality crystals of the tagged and tag‐free variants have been grown. Preliminary X‐ray analyses of tag‐free fragment crystals with (2.2 Å resolution) and without zinc ions (1.7 Å resolution) reveal that the former has at least two zinc ions bound per monomer. |
| doi_str_mv | 10.1107/S1744309107032277 |
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Gerard</creatorcontrib><creatorcontrib>Caffrey, Martin</creatorcontrib><title>Crystallization and preliminary X-ray diffraction analysis of a soluble domain of the putative zinc transporter CzrB from Thermus thermophilus</title><title>Acta crystallographica. Section F, Structural biology and crystallization communications</title><addtitle>Acta Cryst. F</addtitle><description>CzrB is a putative zinc transporter from Thermus thermophilus. The protein is proposed to consist of a hexahelical transmembrane domain with a cytosolic extramembranal C‐terminus. The latter 92‐residue fragment may be expressed free and may function independently of the full‐length integral membrane protein. A 6×His‐tagged form of the water‐soluble fragment has been overexpressed in Escherichia coli and diffraction‐quality crystals of the tagged and tag‐free variants have been grown. Preliminary X‐ray analyses of tag‐free fragment crystals with (2.2 Å resolution) and without zinc ions (1.7 Å resolution) reveal that the former has at least two zinc ions bound per monomer.</description><subject>Amino Acid Sequence</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - metabolism</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - metabolism</subject><subject>cation-diffusion facilitator</subject><subject>Cations, Divalent</subject><subject>CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY</subject><subject>CRYSTALLIZATION</subject><subject>Crystallization Communications</subject><subject>CRYSTALS</subject><subject>CzrB</subject><subject>DIFFUSION</subject><subject>ESCHERICHIA COLI</subject><subject>LENGTH</subject><subject>MEMBRANE PROTEINS</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - metabolism</subject><subject>Molecular Sequence Data</subject><subject>MONOMERS</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>RESOLUTION</subject><subject>Solubility</subject><subject>Thermus thermophilus</subject><subject>WATER</subject><subject>X-RAY DIFFRACTION</subject><subject>ZINC</subject><subject>Zinc - chemistry</subject><subject>Zinc - metabolism</subject><subject>zinc binding</subject><subject>ZINC IONS</subject><subject>zinc transporters</subject><issn>1744-3091</issn><issn>1744-3091</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFks9u1DAQxiMEoqXwAFyQJSRuAf9p7PiC1EZ0AVUgQRFwshxnwhocO9hOYfcheGYSdlWKOPTk0fj3fTMjfUXxkOCnhGDx7D0Rx8cMy7nGjFIhbhWHS6tcerev1QfFvZS-YsyY5PXd4oAILgjj1WHxq4mblLVzdquzDR5p36ExgrOD9Tpu0Kcy6g3qbN9HbfaEdptkEwo90igFN7UOUBcGbf3Sy2tA45Rnu0tAW-sNylH7NIaYIaJmG09RH8OALtYQhyktfBzCuLZuSveLO712CR7s36Piw9mLi-Zlef529ao5OS9NhUlVCs2wML2pWyw1ERUXgI1pOway7iTUrZEtJXUrOsxaTSmQtuuJ5F3HMJa1YUfF853vOLUDdAb8vKNTY7TDfLQK2qp_f7xdqy_hUlHGKsLZbPB4ZxBStioZm8GsTfAeTFaUMo5ZLWfqyX5MDN8nSFkNNhlwTnsIU1K8JmReHt8IUswFp39AsgNNDClF6K92JlgtoVD_hWLWPLp-7F_FPgUzIHfAD-tgc7OjOvl8RlevK0wXbbnT2pTh55VWx2-KCyYq9fHNSr1rVvyiYVxJ9hufKNWH</recordid><startdate>200708</startdate><enddate>200708</enddate><creator>Höfer, Nicole</creator><creator>Kolaj, Olga</creator><creator>Li, Hui</creator><creator>Cherezov, Vadim</creator><creator>Gillilan, Richard</creator><creator>Wall, J. Gerard</creator><creator>Caffrey, Martin</creator><general>Blackwell Publishing Ltd</general><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>7QL</scope><scope>C1K</scope><scope>7X8</scope><scope>OTOTI</scope><scope>5PM</scope></search><sort><creationdate>200708</creationdate><title>Crystallization and preliminary X-ray diffraction analysis of a soluble domain of the putative zinc transporter CzrB from Thermus thermophilus</title><author>Höfer, Nicole ; Kolaj, Olga ; Li, Hui ; Cherezov, Vadim ; Gillilan, Richard ; Wall, J. Gerard ; Caffrey, Martin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5015-7a307cfc8b09a17567e0ccbd3e98d9e8bc9b218b7d03ba22e1bdf196dd30098c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Amino Acid Sequence</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - metabolism</topic><topic>Carrier Proteins - chemistry</topic><topic>Carrier Proteins - metabolism</topic><topic>cation-diffusion facilitator</topic><topic>Cations, Divalent</topic><topic>CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY</topic><topic>CRYSTALLIZATION</topic><topic>Crystallization Communications</topic><topic>CRYSTALS</topic><topic>CzrB</topic><topic>DIFFUSION</topic><topic>ESCHERICHIA COLI</topic><topic>LENGTH</topic><topic>MEMBRANE PROTEINS</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - metabolism</topic><topic>Molecular Sequence Data</topic><topic>MONOMERS</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>RESOLUTION</topic><topic>Solubility</topic><topic>Thermus thermophilus</topic><topic>WATER</topic><topic>X-RAY DIFFRACTION</topic><topic>ZINC</topic><topic>Zinc - chemistry</topic><topic>Zinc - metabolism</topic><topic>zinc binding</topic><topic>ZINC IONS</topic><topic>zinc transporters</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Höfer, Nicole</creatorcontrib><creatorcontrib>Kolaj, Olga</creatorcontrib><creatorcontrib>Li, Hui</creatorcontrib><creatorcontrib>Cherezov, Vadim</creatorcontrib><creatorcontrib>Gillilan, Richard</creatorcontrib><creatorcontrib>Wall, J. 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Gerard</au><au>Caffrey, Martin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystallization and preliminary X-ray diffraction analysis of a soluble domain of the putative zinc transporter CzrB from Thermus thermophilus</atitle><jtitle>Acta crystallographica. Section F, Structural biology and crystallization communications</jtitle><addtitle>Acta Cryst. F</addtitle><date>2007-08</date><risdate>2007</risdate><volume>63</volume><issue>8</issue><spage>673</spage><epage>677</epage><pages>673-677</pages><issn>1744-3091</issn><eissn>1744-3091</eissn><abstract>CzrB is a putative zinc transporter from Thermus thermophilus. The protein is proposed to consist of a hexahelical transmembrane domain with a cytosolic extramembranal C‐terminus. The latter 92‐residue fragment may be expressed free and may function independently of the full‐length integral membrane protein. A 6×His‐tagged form of the water‐soluble fragment has been overexpressed in Escherichia coli and diffraction‐quality crystals of the tagged and tag‐free variants have been grown. Preliminary X‐ray analyses of tag‐free fragment crystals with (2.2 Å resolution) and without zinc ions (1.7 Å resolution) reveal that the former has at least two zinc ions bound per monomer.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>Blackwell Publishing Ltd</pub><pmid>17671365</pmid><doi>10.1107/S1744309107032277</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Acta crystallographica. Section F, Structural biology and crystallization communications, 2007-08, Vol.63 (8), p.673-677 |
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| subjects | Amino Acid Sequence Bacterial Proteins - chemistry Bacterial Proteins - metabolism Carrier Proteins - chemistry Carrier Proteins - metabolism cation-diffusion facilitator Cations, Divalent CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY CRYSTALLIZATION Crystallization Communications CRYSTALS CzrB DIFFUSION ESCHERICHIA COLI LENGTH MEMBRANE PROTEINS Membrane Proteins - chemistry Membrane Proteins - metabolism Molecular Sequence Data MONOMERS Protein Binding Protein Structure, Tertiary RESOLUTION Solubility Thermus thermophilus WATER X-RAY DIFFRACTION ZINC Zinc - chemistry Zinc - metabolism zinc binding ZINC IONS zinc transporters |
| title | Crystallization and preliminary X-ray diffraction analysis of a soluble domain of the putative zinc transporter CzrB from Thermus thermophilus |
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