pH-induced structural changes regulate histidine decarboxylase activity in Lactobacillus 30a
Histidine decarboxylase (HDC) from Lactobacillus 30a produces histamine that is essential to counter waste acids, and to optimize cell growth. The HDC trimer is active at low pH and inactive at neutral to alkaline pH. We have solved the X-ray structure of HDC at pH 8 and revealed the novel mechanism...
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| Veröffentlicht in: | Journal of molecular biology 2001-03, Vol.306 (4), p.727-732 |
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| container_title | Journal of molecular biology |
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| creator | Schelp, Elisabeth Worley, Scott Monzingo, Arthur F Ernst, Stephen Robertus, Jon D |
| description | Histidine decarboxylase (HDC) from
Lactobacillus 30a produces histamine that is essential to counter waste acids, and to optimize cell growth. The HDC trimer is active at low pH and inactive at neutral to alkaline pH. We have solved the X-ray structure of HDC at pH 8 and revealed the novel mechanism of pH regulation. At high pH helix B is unwound, destroying the substrate binding pocket. At acid pH the helix is stabilized, partly through protonation of Asp198 and Asp53 on either side of the molecular interface, acting as a proton trap. In contrast to hemoglobin regulation, pH has a large effect on the tertiary structure of HDC monomers and relatively little or no effect on quaternary structure. |
| doi_str_mv | 10.1006/jmbi.2000.4430 |
| format | Article |
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Lactobacillus 30a produces histamine that is essential to counter waste acids, and to optimize cell growth. The HDC trimer is active at low pH and inactive at neutral to alkaline pH. We have solved the X-ray structure of HDC at pH 8 and revealed the novel mechanism of pH regulation. At high pH helix B is unwound, destroying the substrate binding pocket. At acid pH the helix is stabilized, partly through protonation of Asp198 and Asp53 on either side of the molecular interface, acting as a proton trap. In contrast to hemoglobin regulation, pH has a large effect on the tertiary structure of HDC monomers and relatively little or no effect on quaternary structure.</description><identifier>ISSN: 0022-2836</identifier><identifier>EISSN: 1089-8638</identifier><identifier>DOI: 10.1006/jmbi.2000.4430</identifier><identifier>PMID: 11243783</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Binding Sites ; Crystallography, X-Ray ; helix disorder ; histidine decarboxylase ; Histidine Decarboxylase - chemistry ; Histidine Decarboxylase - metabolism ; Hydrogen-Ion Concentration ; Lactobacillus ; Lactobacillus - enzymology ; Models, Molecular ; pH regulation ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Protons ; pyruvoyl ; X-ray</subject><ispartof>Journal of molecular biology, 2001-03, Vol.306 (4), p.727-732</ispartof><rights>2001 Academic Press</rights><rights>Copyright 2001 Academic Press.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c437t-4b77356623d890f54cd86241ecf26be4086a982f7abad3687e196a7da471a2a13</citedby><cites>FETCH-LOGICAL-c437t-4b77356623d890f54cd86241ecf26be4086a982f7abad3687e196a7da471a2a13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0022283600944309$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11243783$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Schelp, Elisabeth</creatorcontrib><creatorcontrib>Worley, Scott</creatorcontrib><creatorcontrib>Monzingo, Arthur F</creatorcontrib><creatorcontrib>Ernst, Stephen</creatorcontrib><creatorcontrib>Robertus, Jon D</creatorcontrib><title>pH-induced structural changes regulate histidine decarboxylase activity in Lactobacillus 30a</title><title>Journal of molecular biology</title><addtitle>J Mol Biol</addtitle><description>Histidine decarboxylase (HDC) from
Lactobacillus 30a produces histamine that is essential to counter waste acids, and to optimize cell growth. The HDC trimer is active at low pH and inactive at neutral to alkaline pH. We have solved the X-ray structure of HDC at pH 8 and revealed the novel mechanism of pH regulation. At high pH helix B is unwound, destroying the substrate binding pocket. At acid pH the helix is stabilized, partly through protonation of Asp198 and Asp53 on either side of the molecular interface, acting as a proton trap. In contrast to hemoglobin regulation, pH has a large effect on the tertiary structure of HDC monomers and relatively little or no effect on quaternary structure.</description><subject>Binding Sites</subject><subject>Crystallography, X-Ray</subject><subject>helix disorder</subject><subject>histidine decarboxylase</subject><subject>Histidine Decarboxylase - chemistry</subject><subject>Histidine Decarboxylase - metabolism</subject><subject>Hydrogen-Ion Concentration</subject><subject>Lactobacillus</subject><subject>Lactobacillus - enzymology</subject><subject>Models, Molecular</subject><subject>pH regulation</subject><subject>Protein Structure, Quaternary</subject><subject>Protein Structure, Tertiary</subject><subject>Protons</subject><subject>pyruvoyl</subject><subject>X-ray</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1rGzEQQEVpqR2n1x6DTr2tqy9L2mMJTVww9JLcAmJWmrVl1ruOpA31v-8aG3oqOQ0Dbx7DI-QrZ0vOmP6-PzRxKRhjS6Uk-0DmnNm6slraj2TOmBCVsFLPyE3O-4laSWU_kxnnQklj5Zy8HNdV7MPoMdBc0ujLmKCjfgf9FjNNuB07KEh3MZcYYo80oIfUDH9OHWSk4Et8i-VEY0830zI04GPXjZlKBrfkUwtdxi_XuSDPDz-f7tfV5vfjr_sfm8pPX5RKNcbIldZCBluzdqV8sFoojr4VukHFrIbaitZAA0Fqa5DXGkwAZTgI4HJBvl28xzS8jpiLO8Tsseugx2HMzuh6VXPL3gW5sbWquZjA5QX0acg5YeuOKR4gnRxn7hzencO7c3h3Dj8d3F3NY3PA8A-_lp4AewFwCvEWMbnsI_ZT95jQFxeG-D_3X-ZLkl0</recordid><startdate>20010302</startdate><enddate>20010302</enddate><creator>Schelp, Elisabeth</creator><creator>Worley, Scott</creator><creator>Monzingo, Arthur F</creator><creator>Ernst, Stephen</creator><creator>Robertus, Jon D</creator><general>Elsevier Ltd</general><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></search><sort><creationdate>20010302</creationdate><title>pH-induced structural changes regulate histidine decarboxylase activity in Lactobacillus 30a</title><author>Schelp, Elisabeth ; Worley, Scott ; Monzingo, Arthur F ; Ernst, Stephen ; Robertus, Jon D</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c437t-4b77356623d890f54cd86241ecf26be4086a982f7abad3687e196a7da471a2a13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Binding Sites</topic><topic>Crystallography, X-Ray</topic><topic>helix disorder</topic><topic>histidine decarboxylase</topic><topic>Histidine Decarboxylase - chemistry</topic><topic>Histidine Decarboxylase - metabolism</topic><topic>Hydrogen-Ion Concentration</topic><topic>Lactobacillus</topic><topic>Lactobacillus - enzymology</topic><topic>Models, Molecular</topic><topic>pH regulation</topic><topic>Protein Structure, Quaternary</topic><topic>Protein Structure, Tertiary</topic><topic>Protons</topic><topic>pyruvoyl</topic><topic>X-ray</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schelp, Elisabeth</creatorcontrib><creatorcontrib>Worley, Scott</creatorcontrib><creatorcontrib>Monzingo, Arthur F</creatorcontrib><creatorcontrib>Ernst, Stephen</creatorcontrib><creatorcontrib>Robertus, Jon D</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schelp, Elisabeth</au><au>Worley, Scott</au><au>Monzingo, Arthur F</au><au>Ernst, Stephen</au><au>Robertus, Jon D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>pH-induced structural changes regulate histidine decarboxylase activity in Lactobacillus 30a</atitle><jtitle>Journal of molecular biology</jtitle><addtitle>J Mol Biol</addtitle><date>2001-03-02</date><risdate>2001</risdate><volume>306</volume><issue>4</issue><spage>727</spage><epage>732</epage><pages>727-732</pages><issn>0022-2836</issn><eissn>1089-8638</eissn><abstract>Histidine decarboxylase (HDC) from
Lactobacillus 30a produces histamine that is essential to counter waste acids, and to optimize cell growth. The HDC trimer is active at low pH and inactive at neutral to alkaline pH. We have solved the X-ray structure of HDC at pH 8 and revealed the novel mechanism of pH regulation. At high pH helix B is unwound, destroying the substrate binding pocket. At acid pH the helix is stabilized, partly through protonation of Asp198 and Asp53 on either side of the molecular interface, acting as a proton trap. In contrast to hemoglobin regulation, pH has a large effect on the tertiary structure of HDC monomers and relatively little or no effect on quaternary structure.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>11243783</pmid><doi>10.1006/jmbi.2000.4430</doi><tpages>6</tpages></addata></record> |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Binding Sites Crystallography, X-Ray helix disorder histidine decarboxylase Histidine Decarboxylase - chemistry Histidine Decarboxylase - metabolism Hydrogen-Ion Concentration Lactobacillus Lactobacillus - enzymology Models, Molecular pH regulation Protein Structure, Quaternary Protein Structure, Tertiary Protons pyruvoyl X-ray |
| title | pH-induced structural changes regulate histidine decarboxylase activity in Lactobacillus 30a |
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