1bro: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
 
Line 3: Line 3:
<StructureSection load='1bro' size='340' side='right'caption='[[1bro]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
<StructureSection load='1bro' size='340' side='right'caption='[[1bro]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1bro]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_10762 Atcc 10762]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BRO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1BRO FirstGlance]. <br>
<table><tr><td colspan='2'>[[1bro]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Kitasatospora_aureofaciens Kitasatospora aureofaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BRO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BRO FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BPOA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1894 ATCC 10762])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1bro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bro OCA], [http://pdbe.org/1bro PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bro RCSB], [http://www.ebi.ac.uk/pdbsum/1bro PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bro ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bro OCA], [https://pdbe.org/1bro PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bro RCSB], [https://www.ebi.ac.uk/pdbsum/1bro PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bro ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/BPOA2_STRAU BPOA2_STRAU]] May be a chlorinating enzyme involved in 7-chlorotetracycline biosynthesis.  
[https://www.uniprot.org/uniprot/BPOA2_KITAU BPOA2_KITAU] May be a chlorinating enzyme involved in 7-chlorotetracycline biosynthesis.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 19: Line 19:
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bro ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bro ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of the bromoperoxidase A2 from Streptomyces aureofaciens (ATCC 10762) has been determined by isomorphous replacement and refined to 2.05 A resolution with an R-value of 18.4%. The enzyme catalyzes the bromination of organic compounds in the presence of bromide and peroxide. The structure confirms the absence of cofactors such as metal ions or haem groups and shows the general topology of the alpha/beta hydrolase fold. The active centre is at the end of a deep pocket and includes a catalytic triad of Ser 98, Asp 228 and His 257. The active centre is connected by a narrow tunnel to a second pocket on the enzyme surface.
The metal-ion-free oxidoreductase from Streptomyces aureofaciens has an alpha/beta hydrolase fold.,Hecht HJ, Sobek H, Haag T, Pfeifer O, van Pee KH Nat Struct Biol. 1994 Aug;1(8):532-7. PMID:7664081<ref>PMID:7664081</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1bro" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Haloperoxidase|Haloperoxidase]]
*[[Haloperoxidase|Haloperoxidase]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 10762]]
[[Category: Kitasatospora aureofaciens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Haag, T]]
[[Category: Haag T]]
[[Category: Hecht, H J]]
[[Category: Hecht HJ]]
[[Category: Pee, K H.Van]]
[[Category: Pfeifer O]]
[[Category: Pfeifer, O]]
[[Category: Sobek H]]
[[Category: Sobek, H]]
[[Category: Van Pee KH]]
[[Category: Alpha/beta hydrolase fold]]
[[Category: Antibiotic biosynthesis]]
[[Category: Haloperoxidase]]
[[Category: Oxidoreductase]]
[[Category: Peroxidase]]

Latest revision as of 06:38, 7 February 2024

BROMOPEROXIDASE A2

1bro, resolution 2.05Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1bro&oldid=4040786"