<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Seki K</submitter><funding>Kowa Life Science Foundation</funding><funding>Japan Agency for Medical Research and Development</funding><funding>Japan Society for the Promotion of Science</funding><pagination>111012</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12796733</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>302(1)</volume><pubmed_abstract>Streptococcus pyogenes causes a range of infectious diseases. In an era of increasing antibiotic resistance, new antimicrobial strategies targeting virulence factors, rather than essential survival mechanisms, are being explored. A key virulence factor in S. pyogenes is the bacterial iron acquisition system, because iron is essential but limited in the host due to sequestration by proteins like hemoglobin. The bacteria S. pyogenes possesses the Shr protein that acquires heme from host hemoglobin and transfers it to Shp, a membrane proximity protein. Shr comprises multiple domains, including two NEAr-Transporter (NEAT) domains that directly bind to heme. While structural information of NEAT domains from other bacteria are available, the structure of NEAT domains from Shr remains unknown. In</pubmed_abstract><journal>The Journal of biological chemistry</journal><pubmed_title>Structural basis for heme binding by the Shr protein from Streptococcus pyogenes.</pubmed_title><pmcid>PMC12796733</pmcid><funding_grant_id>JP23ama121031</funding_grant_id><funding_grant_id>24K18262</funding_grant_id><funding_grant_id>JP22ama121033</funding_grant_id><pubmed_authors>Caaveiro JMM</pubmed_authors><pubmed_authors>Nagatoishi S</pubmed_authors><pubmed_authors>Yanaka S</pubmed_authors><pubmed_authors>Seki K</pubmed_authors><pubmed_authors>Nakakido M</pubmed_authors><pubmed_authors>Tsumoto K</pubmed_authors><pubmed_authors>Senoo A</pubmed_authors></additional><is_claimable>false</is_claimable><name>Structural basis for heme binding by the Shr protein from Streptococcus pyogenes.</name><description>Streptococcus pyogenes causes a range of infectious diseases. In an era of increasing antibiotic resistance, new antimicrobial strategies targeting virulence factors, rather than essential survival mechanisms, are being explored. A key virulence factor in S. pyogenes is the bacterial iron acquisition system, because iron is essential but limited in the host due to sequestration by proteins like hemoglobin. The bacteria S. pyogenes possesses the Shr protein that acquires heme from host hemoglobin and transfers it to Shp, a membrane proximity protein. Shr comprises multiple domains, including two NEAr-Transporter (NEAT) domains that directly bind to heme. While structural information of NEAT domains from other bacteria are available, the structure of NEAT domains from Shr remains unknown. In</description><dates><release>2025-01-01T00:00:00Z</release><publication>2025 Dec</publication><modification>2026-06-09T05:35:41.863Z</modification><creation>2026-06-09T03:07:39.747Z</creation></dates><accession>S-EPMC12796733</accession><cross_references><pubmed>41354341</pubmed><doi>10.1016/j.jbc.2025.111012</doi></cross_references></HashMap>